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Database: UniProt
Entry: O34720
LinkDB: O34720
Original site: O34720 
ID   YJGC_BACSU              Reviewed;         985 AA.
AC   O34720; Q796P0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   10-APR-2019, entry version 128.
DE   RecName: Full=Probable oxidoreductase YjgC;
DE            EC=1.-.-.-;
GN   Name=yjgC; OrderedLocusNames=BSU12160;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9579062; DOI=10.1099/00221287-144-4-877;
RA   Rivolta C., Soldo B., Lazarevic V., Joris B., Mauel C., Karamata D.;
RT   "A 35.7 kb DNA fragment from the Bacillus subtilis chromosome
RT   containing a putative 12.3 kb operon involved in hexuronate catabolism
RT   and a perfectly symmetrical hypothetical catabolite-responsive
RT   element.";
RL   Microbiology 144:877-884(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 4 [4Fe-4S] clusters. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC       Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide)
CC       (Mo-bis-MGD) cofactor per subunit. {ECO:0000250};
CC   -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC       molybdopterin-containing oxidoreductase family. {ECO:0000305}.
DR   EMBL; AF015825; AAC46312.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13073.1; -; Genomic_DNA.
DR   PIR; E69850; E69850.
DR   RefSeq; NP_389098.1; NC_000964.3.
DR   RefSeq; WP_003245240.1; NZ_JNCM01000035.1.
DR   ProteinModelPortal; O34720; -.
DR   SMR; O34720; -.
DR   IntAct; O34720; 1.
DR   STRING; 224308.BSU12160; -.
DR   PaxDb; O34720; -.
DR   PRIDE; O34720; -.
DR   EnsemblBacteria; CAB13073; CAB13073; BSU12160.
DR   GeneID; 939396; -.
DR   KEGG; bsu:BSU12160; -.
DR   PATRIC; fig|224308.179.peg.1314; -.
DR   eggNOG; ENOG4108IEG; Bacteria.
DR   eggNOG; COG3383; LUCA.
DR   HOGENOM; HOG000031440; -.
DR   InParanoid; O34720; -.
DR   KO; K00123; -.
DR   OMA; MESAMRD; -.
DR   PhylomeDB; O34720; -.
DR   BioCyc; BSUB:BSU12160-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006478; Formate_DH_asu.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   TIGRFAMs; TIGR01591; Fdh-alpha; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS51839; 4FE4S_HC3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding;
KW   Molybdenum; Oxidoreductase; Reference proteome; Repeat.
FT   CHAIN         1    985       Probable oxidoreductase YjgC.
FT                                /FTId=PRO_0000380112.
FT   DOMAIN        3     79       2Fe-2S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   DOMAIN       79    119       4Fe-4S His(Cys)3-ligated-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01184}.
FT   DOMAIN      139    170       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      182    211       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      258    314       4Fe-4S Mo/W bis-MGD-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01004}.
FT   METAL        37     37       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        48     48       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        51     51       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        63     63       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        95     95       Iron-sulfur 2 (4Fe-4S); via tele
FT                                nitrogen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01184}.
FT   METAL        99     99       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU01184}.
FT   METAL       102    102       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU01184}.
FT   METAL       109    109       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU01184}.
FT   METAL       148    148       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       151    151       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       154    154       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       158    158       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       191    191       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       194    194       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       197    197       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       201    201       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       265    265       Iron-sulfur 5 (4Fe-4S). {ECO:0000250}.
FT   METAL       268    268       Iron-sulfur 5 (4Fe-4S). {ECO:0000250}.
FT   METAL       272    272       Iron-sulfur 5 (4Fe-4S). {ECO:0000250}.
FT   METAL       300    300       Iron-sulfur 5 (4Fe-4S). {ECO:0000250}.
SQ   SEQUENCE   985 AA;  109789 MW;  83A3C765CDB362AD CRC64;
     MAGKKTITIN GVEMEASEEQ TVLQLLNNSS IEVPQVCYHP SLGPIETCDT CIVSINGELK
     RSCSAELKDG DVIDTLSPDV KKAQVIGMDK ILYNHELYCT VCDYNNGGCE IHNTVKEMKI
     NHQSIPFDHK PYHKDESHPF YRYDPDQCIL CGRCVEACQD VQVTETLTID WERKRPRVIW
     DNDVPINESS CVSCGHCSTV CPCNAMMEKG MEGEAGYLTG INNETLRPMI EITKGVETGY
     GSILAISDME SAMRDERIKK TKTVCTYCGV GCSFDVWTKG RDILKVEPQE EAPANGISTC
     VKGKFGWDFV NSEERLTKPL IREGDHFREA EWEEALLLIA SKFTELKEAF GPDSLAFITS
     SKCTNEESYL MQKLARGVIG TNNVDNCSRY CQSPATAGLF RTVGYGGDSG SITDIAQADL
     VLIIGSNTSE SHPVLSTRIK RAHKLRGQKV IVADIRKHEM AERSDLFVQP RAGSDIVWLN
     AIAKYLIENG KADERFLRER VNGRDEYVKS LAPYTLEYAE EKTGIDQETL IQMAEMIGQA
     DSVCALWAMG VTQHIGGSDT STAISNLLLV TGNYGKPGAG SYPLRGHNNV QGASDFGSMP
     DRLPGYEKVT DEQVRQKYER VWGVPLPKEP GMTNHEMIEK IHSGQLKAMY VKGEEMGLVD
     SNINHVHAAY EKLDFFVVQD IFLSRTAEFA DVVLPASPSL EKEGTFTNTE RRIQRLYQVF
     EPLGESKPDW QIIMEVANKL GAGWLYEHPA DIMEEAAKLS PIYAGVTYER LEGYNSLQWP
     VNADGKDSPL LFTERFPFPD GKAILYPVQW TEPKEFGEEY DIHVNNGRLL EHFHEGNLTY
     KSKGISEKTP EVFLEISPEL AAERGIQDGT LVRLTSPFGN VKVKCLITDR VKGKEVYLPM
     NDSGEAAINL LTGSHADKDT DTPAYKETSA KMEILKHDGI SPLPKINHRN GNPQPQIGVQ
     VHKKWARKDY IFPGDAVKRG MGHNG
//
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