Y2900_MYCTO
ID Y2900_MYCTO Reviewed; 779 AA.
AC P9WJP8; L0TDW4; P65408; Q10821;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Uncharacterized oxidoreductase MT2968;
DE EC=1.-.-.-;
GN OrderedLocusNames=MT2968;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
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) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AE000516; AAK47294.1; -; Genomic_DNA.
DR PIR; G70926; G70926.
DR RefSeq; WP_003899532.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WJP8; -.
DR SMR; P9WJP8; -.
DR EnsemblBacteria; AAK47294; AAK47294; MT2968.
DR KEGG; mtc:MT2968; -.
DR PATRIC; fig|83331.31.peg.3208; -.
DR HOGENOM; CLU_000422_16_1_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR CDD; cd02787; MopB_CT_ydeP; 1.
DR CDD; cd02767; MopB_ydeP; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037951; MopB_CT_YdeP.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR010046; Mopterin_OxRdtse_a_bac.
DR InterPro; IPR041953; YdeP_MopB.
DR PANTHER; PTHR43105:SF4; PTHR43105:SF4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR01701; Fdhalpha-like; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase.
FT CHAIN 1..779
FT /note="Uncharacterized oxidoreductase MT2968"
FT /id="PRO_0000427792"
FT BINDING 72
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 779 AA; 84566 MW; 382FB089071E8E54 CRC64;
MYVEAVRWQR SAASRDVLAD YDEQAVTVAP RKREAAGVRA VMVSLQRGMQ QMGALRTAAA
LARLNQRNGF DCPGCAWPEE PGGRKLAEFC ENGAKAVAEE ATKRTVTAEF FARHSVAELS
AKPEYWLSQQ GRLAHPMVLR PGDDHYRPIS WDAAYQLIAE QLNGLDSPDR AVFYTSGRTS
NEAAFCYQLL VRSFGTNNLP DCSNMCHESS GAALTDSIGI GKGSVTIGDV EHADLIVIAG
QNPGTNHPRM LSVLGKAKAN GAKIIAVNPL PEAGLIRFKD PQKVNGVVGH GIPIADEFVQ
IRLGGDMALF AGLGRLLLEA EERVPGSVVD RSFVDNHCAG FDGYRRRTLQ VGLDTVMDAT
GIELAQLQRV AAMLMASQRT VICWAMGLTQ HAHAVATIGE VTNVLLLRGM IGKPGAGVCP
VRGHSNVQGD RTMGIWEKMP EQFLAALDRE FGITSPRAHG FDTVAAIRAM RDGRVSVFMG
MGGNFASATP DTAVTEAALR RCALTVQVST KLNRSHLVHG ATALILPTLG RTDRDTRNGR
KQLVSVEDSM SMVHLSRGSL HPPSDQVRSE VQIICQLARA LFGPGHPVPW ERFADDYDTI
RDAIAAVVPG CDDYNHKVRV PDGFQLPHPP RDAREFRTST GKANFAVNPL QWVPVPPGRL
VLQTLRSHDQ YNTTIYGLDD RYRGVKGGRR VVFINPADIE TFGLTAGDRV DLVSEWTDGQ
GGLQERRAKD FLVVAYSTPV GNAAAYYPET NPLVPLDHTA AQSNTPVSKA IIVRLEPTA