ID A2SGH9_METPP Unreviewed; 1268 AA.
AC A2SGH9;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Respiratory nitrate reductase alpha subunit apoprotein {ECO:0000313|EMBL:ABM94668.1};
GN OrderedLocusNames=Mpe_A1708 {ECO:0000313|EMBL:ABM94668.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM94668.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM94668.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP000555; ABM94668.1; -; Genomic_DNA.
DR RefSeq; WP_011829305.1; NC_008825.1.
DR AlphaFoldDB; A2SGH9; -.
DR STRING; 420662.Mpe_A1708; -.
DR KEGG; mpt:Mpe_A1708; -.
DR eggNOG; COG5013; Bacteria.
DR HOGENOM; CLU_000422_14_1_4; -.
DR Proteomes; UP000000366; Chromosome.
DR GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR GO; GO:0042126; P:nitrate metabolic process; IEA:InterPro.
DR CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR CDD; cd02750; MopB_Nitrate-R-NarG-like; 1.
DR Gene3D; 3.40.50.12440; -; 1.
DR Gene3D; 4.10.1200.10; nitrate reductase tail; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-like.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR006468; NarG.
DR InterPro; IPR028189; Nitr_red_alph_N.
DR InterPro; IPR044906; Nitr_red_alph_N_sf.
DR NCBIfam; TIGR01580; narG; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR PANTHER; PTHR43105:SF2; RESPIRATORY NITRATE REDUCTASE 2 ALPHA CHAIN; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF14710; Nitr_red_alph_N; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000366}.
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1268 AA; 141717 MW; C12EE86123B5D0E5 CRC64;
MSHFLDRLTH FKLPQEAFSG DHGRTTGEDR TWEDAYRNRW AHDKIVRSTH GVNCTGSCSW
KIYVKGGIVT WETQQTDYPR TRADLPNHEP RGCARGASYS WYLYSANRVK YPMVRGRLLE
AWRAALKVSK TPVDAWTLVV ENEATRRGYQ KVRGMGGFVR SSWDEVNQLI AAANVYTIKK
YGPDRVIGFS PIPAMSMVSY AAGSRYLSLI GGVCMSFYDW YCDLPPASPQ IWGEQTDVPE
SADWYNSTYI IAWGSNVPQT RTPDAHFFTE VRYKGAKTVA VTPDYAEVSK LADLWLHPKQ
GTDAALAMAM GHVALKEFFF DRRAAYFDDY ARRYTDLPLL VLLEEKRLPD GRTVLAPGRY
LRASDFNGKL GQTNNPDWKT VAFDTVGKAV LPNGSIGFRW GAEGRDDAGK WNLEAKEARH
DSDVKLKLSV LEDGAQAHEV VDVAFPYFAG AEVPHFTPSP QAGGELNQAR VPAVRLRLGK
EGEERHALVA TVFDLQAAQY GIDRGLGSGA KSYDDDAPYT PAWQERITGV PRAQVITVAR
EFAANAEKTR GKSMVIIGAA MNHWYHADMN YRGVINLLMM CGCIGQSGGG WAHYVGQEKL
RPQTGWVPLA FATDWIRPPR QQNSTSFFYA HTDQWRYEKL GVESILSPLF KTEADKGKFG
GSLIDYNVRA ERMGWLPSAP QLKTNPLQVV KDAAAAGQDA KDYAVRALQD GRLEMSCEDP
DAPQNWPRNL FVWRSNLLGS SGKGHEYFCK HLLGTENGVQ GKDLGRDDAK PHEVKWHEHA
PEGKLDLVVT LDFRMSTTCL YSDIVLPTAS WYEKNDLNTS DMHPFIHPLS AAVDPVWQAR
SDWEIYKGFA KAFSEVCVGH LGVEKELVLT PMQHDTPAEL AQGWDFKEWR KGECELIPGK
TAPVMTVVER DYPGVFKRFT SLGPLMTKVG NGGKGIAWKT EVEVKQLAEL NGVDAEGRPR
IVSDIDACEV ILQLAPETNG HVAVKAWEAL GKITGRDHTH LALHREDEKI RYRDVQAQPR
KIISSPTWSG LESEKVSYNA GYTNVHELIP WRTLTGRQQF YQDHPWMVAF GEGFSSYRPP
VDLKTTAAML GAKPNGQKEV VLNFITPHQK WGIHSTYSDN LMMLTLNRGG PVIWLSEEDA
KAAGIADNDW VELFNVNGAI SARAVVSQRV KPGMTMMYHA QEKIINAPGS EITGVRGGIH
NSVTRIVTKP THMIGGYAQY SYGFNYYGTI GTNRDEFVVV RKMAKVDWLD TPADDHLAAV
YQAQGENP
//
