GLPC_HAEIN
ID GLPC_HAEIN Reviewed; 426 AA.
AC P43801;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit C;
DE Short=G-3-P dehydrogenase;
GN Name=glpC; OrderedLocusNames=HI_0683;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Electron transfer protein; may also function as the membrane
CC anchor for the GlpAB dimer. {ECO:0000250}.
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 {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Note=Loosely bound to the cytoplasmic
CC membrane often occurring in vesicles associated with fumarate
CC reductase. {ECO:0000250}.
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DR EMBL; L42023; AAC22343.1; -; Genomic_DNA.
DR PIR; C64086; C64086.
DR RefSeq; NP_438843.1; NC_000907.1.
DR RefSeq; WP_005694608.1; NC_000907.1.
DR AlphaFoldDB; P43801; -.
DR STRING; 71421.HI_0683; -.
DR EnsemblBacteria; AAC22343; AAC22343; HI_0683.
DR KEGG; hin:HI_0683; -.
DR PATRIC; fig|71421.8.peg.714; -.
DR eggNOG; COG0247; Bacteria.
DR HOGENOM; CLU_023081_7_1_6; -.
DR OMA; CGMPKLE; -.
DR PhylomeDB; P43801; -.
DR BioCyc; HINF71421:G1GJ1-718-MON; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IEA:InterPro.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW 4Fe-4S; Cell inner membrane; Cell membrane; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..426
FT /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT C"
FT /id="PRO_0000159261"
FT DOMAIN 21..53
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 67..99
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 32
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 426 AA; 48069 MW; A6EA5F33C6C4FC3C CRC64;
MDNNIQRLID SAKQSLNSPE SYKYIDESFE SCIKCTACTA VCPVSRNNPL YPGPKQSGPD
GERLRLKSAE LYDEALKYCT NCKRCEVACP SDVKIGDLIV RARNNHLAQS KKPLMNKLRD
AILSNTDVMG KINTPLAPIV NTITGLKATK FMLEKTLNIS KKRTLPKYAF GTFRSWYMKN
ALQDQQKFER KVAYFHGCYV NYNNPQLGKE FLKVFNAMNI GVMLLEKEKC CGLPLMVNGF
PNRARNIAQF NTDYIGKMVD ENGIDVISEA SSCSLNLRDE YHHILGIDNA KVRPHIHMVT
PFLYQLFKEG KTLPLKPLKL RVAYHTACHV DKAGWAPYTL EVLKKIPSLE IIMLPSQCCG
IAGTYGFKSE NYEISQSIGK NLFDNINEGG FDYVISECQT CKWQIDMSSN VTCIHPLTLL
CMSMDA
