GLPC_ECOLI
ID GLPC_ECOLI Reviewed; 396 AA.
AC P0A996; P13034; P76927; P77679;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit C;
DE Short=G-3-P dehydrogenase;
GN Name=glpC; OrderedLocusNames=b2243, JW2237;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12;
RX PubMed=3286606; DOI=10.1128/jb.170.6.2448-2456.1988;
RA Cole S.T., Eiglmeier K., Ahmed S., Honore N., Elmes L., Anderson W.F.,
RA Weiner J.H.;
RT "Nucleotide sequence and gene-polypeptide relationships of the glpABC
RT operon encoding the anaerobic sn-glycerol-3-phosphate dehydrogenase of
RT Escherichia coli K-12.";
RL J. Bacteriol. 170:2448-2456(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Electron transfer protein; may also function as the membrane
CC anchor for the GlpAB dimer.
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC route): step 1/1.
CC -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of GlpC.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
CC Note=Loosely bound to the cytoplasmic membrane often occurring in
CC vesicles associated with fumarate reductase.
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DR EMBL; M20938; AAA83866.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75303.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16062.1; -; Genomic_DNA.
DR PIR; A64995; DEECNC.
DR RefSeq; NP_416746.1; NC_000913.3.
DR RefSeq; WP_001000379.1; NZ_LN832404.1.
DR AlphaFoldDB; P0A996; -.
DR BioGRID; 4262942; 101.
DR BioGRID; 851076; 1.
DR ComplexPortal; CPX-4841; Anaerobic glycerol-3-phosphate dehydrogenase complex.
DR DIP; DIP-35835N; -.
DR IntAct; P0A996; 20.
DR STRING; 511145.b2243; -.
DR jPOST; P0A996; -.
DR PaxDb; P0A996; -.
DR PRIDE; P0A996; -.
DR EnsemblBacteria; AAC75303; AAC75303; b2243.
DR EnsemblBacteria; BAA16062; BAA16062; BAA16062.
DR GeneID; 946735; -.
DR KEGG; ecj:JW2237; -.
DR KEGG; eco:b2243; -.
DR PATRIC; fig|511145.12.peg.2332; -.
DR EchoBASE; EB0388; -.
DR eggNOG; COG0247; Bacteria.
DR HOGENOM; CLU_023081_7_1_6; -.
DR InParanoid; P0A996; -.
DR OMA; FQRCCGA; -.
DR PhylomeDB; P0A996; -.
DR BioCyc; EcoCyc:ANGLYC3PDEHYDROGSUBUNITC-MON; -.
DR BioCyc; MetaCyc:ANGLYC3PDEHYDROGSUBUNITC-MON; -.
DR UniPathway; UPA00618; UER00673.
DR PRO; PR:P0A996; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
DR GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
DR GO; GO:0022900; P:electron transport chain; IDA:EcoCyc.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IC:ComplexPortal.
DR Gene3D; 1.10.1060.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004017; Cys_rich_dom.
DR InterPro; IPR017753; G3P_DH_GlpC_su.
DR InterPro; IPR009051; Helical_ferredxn.
DR Pfam; PF02754; CCG; 2.
DR Pfam; PF13183; Fer4_8; 1.
DR TIGRFAMs; TIGR03379; glycerol3P_GlpC; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..396
FT /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT C"
FT /id="PRO_0000159259"
FT DOMAIN 2..29
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 45..76
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 9
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 169
FT /note="C -> V (in Ref. 1; AAA83866)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="L -> V (in Ref. 1; AAA83866)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 44108 MW; 1DC9203332B6F2F2 CRC64;
MNDTSFENCI KCTVCTTACP VSRVNPGYPG PKQAGPDGER LRLKDGALYD EALKYCINCK
RCEVACPSDV KIGDIIQRAR AKYDTTRPSL RNFVLSHTDL MGSVSTPFAP IVNTATSLKP
VRQLLDAALK IDHRRTLPKY SFGTFRRWYR SVAAQQAQYK DQVAFFHGCF VNYNHPQLGK
DLIKVLNAMG TGVQLLSKEK CCGVPLIANG FTDKARKQAI TNVESIREAV GVKGIPVIAT
SSTCTFALRD EYPEVLNVDN KGLRDHIELA TRWLWRKLDE GKTLPLKPLP LKVVYHTPCH
MEKMGWTLYT LELLRNIPGL ELTVLDSQCC GIAGTYGFKK ENYPTSQAIG APLFRQIEES
GADLVVTDCE TCKWQIEMST SLRCEHPITL LAQALA
