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3.B.1.1.7
Na+-pumping glutaconyl-CoA decarboxylase, Gcd, with subunits A4/B2/C11/C21/D2 (The stoichiometry of the subunits is given by the subscripts.). Gcd drives the endergonic translocation of Na+ across the membrane with the exergonic decarboxylation of glutaconyl-CoA (ΔG0’ ≈−30 kJ/mol) to crotonyl-CoA. Vitt et al. 2020 reported on the molecular characterization of Gcd from Clostridium symbiosum. The subunit composition is four GcdA (65 kDa), two GcdB (35 kDa), one GcdC1 (15 kDa), one GcdC2 (14 kDa), and two GcdD (10 kDa). Low-resolution structural information was achieved by electron microscopic (EM) measurements, which resulted in a 3D reconstruction model based on negative-stained particles. The Gcd structure is built up of a membrane-spanning base primarily composed of the GcdB dimer and a solvent-exposed head with the GcdA tetramer as the major component. These two globular parts are bridged by a linker presumably built up of segments of GcdC1, GcdC2 and the 2 GcdDs. The structure of the highly mobile Gcd complex represents a template for the global architecture of the Bdc family (Vitt et al. 2020).

Accession Number:B7TVP1
Protein Name:Glutaconyl-CoA decarboxylase alpha subunit
Length:588
Molecular Weight:64961.00
Species:Clostridium symbiosum [1512]
Substrate sodium(1+)

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Structure:
3GF3   3GF7   3GLM   3GMA     

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FASTA formatted sequence
1:	MNMYSMPGYF QNMPTIGKEL VNPNPENEQE IKAVESDIHE SIKKALDAGI TSEEKLNERG 
61:	QLSAMQRINA LIDPGTWCPL NSLFNPENNK FGTTNIVNGL GRVDGKWVYI VASDNKKMAG 
121:	AWVPGQAENL IRCSDAAKMM HLPLIYLLNC SGVEFPNQDK VYPNRRGGGT PFFRNSELNQ 
181:	LGIPVIVGIY GTNPAGGGYH SISPTILIAH QDANMAVGGA GILSGMNPKG YIDDEAAEQI 
241:	IAAQIENSKL KVPAPGSVPI HYDETGFFRE VYQNDLGVID GIKKYISYLP AYNLEFFRVD 
301:	TPKAPQLPAE DLYSIIPMNQ KRPYDIYEVI ARLFDNSEFS EYKKGYGPEM VTGLAKVNGL 
361:	LVGVIANVQG LLMNYPEYKQ NSVGIGGKLY RQGLIKMNEF VTLCARDRIP LIWLQDTTGI 
421:	DVGDEAEKAE LLGLGQSLIY SIENSKLPSL EITIRKASAA AHYVLGGPQG NNTNVFSIGT 
481:	GACEYYVMPG ETAANAMYSR KLVKAKKAGE DLQPIIGKMN DMIQMYTDKS RPKYCTEKGM 
541:	VDEIVDMTEV RPYIQAFTEA AYQNPQSICP MHQMLTPRST REFETFGK