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Database: UniProt
Entry: P43801
LinkDB: P43801
Original site: P43801 
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   10-APR-2019, entry version 115.
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.,
RA   Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA   Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA   Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA   Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA   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
CC       membrane anchor for the GlpAB dimer. {ECO:0000250}.
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate
CC       (anaerobic 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};
CC       Peripheral membrane protein {ECO:0000250}. Note=Loosely bound to
CC       the cytoplasmic membrane often occurring in vesicles associated
CC       with fumarate reductase. {ECO:0000250}.
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   ProteinModelPortal; P43801; -.
DR   STRING; 71421.HI_0683; -.
DR   PRIDE; P43801; -.
DR   EnsemblBacteria; AAC22343; AAC22343; HI_0683.
DR   GeneID; 949971; -.
DR   KEGG; hin:HI0683; -.
DR   PATRIC; fig|71421.8.peg.714; -.
DR   eggNOG; ENOG4105CHG; Bacteria.
DR   eggNOG; COG0247; LUCA.
DR   KO; K00113; -.
DR   OMA; VAYHTPC; -.
DR   PhylomeDB; P43801; -.
DR   BioCyc; HINF71421:G1GJ1-718-MONOMER; -.
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   SUPFAM; SSF46548; SSF46548; 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; Complete proteome;
KW   Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Reference proteome; Repeat; Transport.
FT   CHAIN         1    426       Anaerobic glycerol-3-phosphate
FT                                dehydrogenase subunit C.
FT                                /FTId=PRO_0000159261.
FT   DOMAIN       21     53       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       67     99       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        32     32       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        35     35       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        38     38       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        42     42       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        79     79       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        82     82       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        85     85       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        89     89       Iron-sulfur 1 (4Fe-4S). {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
//
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