ID Q31GG9_HYDCU Unreviewed; 907 AA.
AC Q31GG9;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Assimilatory nitrate reductase (NADH) alpha subunit apoprotein {ECO:0000313|EMBL:ABB41754.1};
DE EC=1.7.1.1 {ECO:0000313|EMBL:ABB41754.1};
GN OrderedLocusNames=Tcr_1159 {ECO:0000313|EMBL:ABB41754.1};
OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS crunogena).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=317025 {ECO:0000313|EMBL:ABB41754.1};
RN [1] {ECO:0000313|EMBL:ABB41754.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=XCL-2 {ECO:0000313|EMBL:ABB41754.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Scott K.M., Sievert S., Kerfeld C.,
RA Freyermuth S., Dobrinski K., Boller A., Fitzpatrick K., Thoma P., Moore J.,
RA Richardson P.;
RT "Complete sequence of Thiomicrospira crunogena XCL-2.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily.
CC {ECO:0000256|ARBA:ARBA00008747}.
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DR EMBL; CP000109; ABB41754.1; -; Genomic_DNA.
DR AlphaFoldDB; Q31GG9; -.
DR STRING; 317025.Tcr_1159; -.
DR KEGG; tcx:Tcr_1159; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG1251; Bacteria.
DR HOGENOM; CLU_000422_13_4_6; -.
DR OrthoDB; 9810782at2; -.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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:0009703; F:nitrate reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR CDD; cd02754; MopB_Nitrate-R-NapA-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 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.
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 Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABB41754.1}.
FT DOMAIN 9..71
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 907 AA; 100333 MW; DE1526358542412B CRC64;
MNRPVFLNPE DVETTCPYCG VGCGMTVSSK APSTESDSFE VKVKGSPSHR ANYGKLCVKG
SSAGETVDFS GRMLHPQIDG NIVDWETALN DVAKTFQKTI SEYGPDSVAF YVSGQFLTED
YYVANKLIKG FMGTANIDTN SRLCMASAVV GYKRAFGSDT VPCCYEDLEH ADLITLVGSN
TAWAHPIIYQ RIAAAKKKNP KLKIVVVDPR KTATCDIADL HLAIKPGMDA ALFNGLLAYL
NQQNALDLDY IQKHTEGFES ALQKANELQG NVSDLATQCD LNETDLRQWL DWATYTPKMV
TMYSQGINQS SSGVDKSNAI INCHLATGRI GKEGMGPFSI TGQPNAMGGR EVGGLANQLA
AHMDFSDSEN IDRVARFWQA ENMAQQNGLK AVDLFHAVGE GKIKAIWIMN TNPVVSMPDA
DNVKRALEKC DYVVVQDCMQ DTDTTRVANV LLPATTWGET DGAVTNSDRT ISIQRQFMQG
PENARPDWWI LSEVAKKMGW AHAFNYDSAV DIFREHAQLS GFENNGSRDF DISAFANISK
QEYAHFKPIQ WPVNVSAPNG TQRMFSDGCF FTPSKKAQFI AITPYAPLSQ QTKDKPYVLN
TGRVRDQWHT MTRTAKTAKL MAHKNEPYIT LHPDDARIQR LSEGDLVRVS NELGQLIGRV
EVSDSQRRGE IFVPIHWTSQ YASHGRVDSL IKANVDPLSG QPESKHATVT IERYSAQWQG
FILSRTAINP ELFDDDYWVK ITGKHFYRYE IASERAIKNA HAWAKTILSS SENTEWIEYD
DASCKQYRAA LIKNDQLQKV FFMAEDHKMP SRDWLGHLFS ATELSPIERR SLLAGKASGA
KDPGRTICSC FGVGINTIIE AIEAQNLVSV EAIGQALKAG TNCGSCVPEL TEILAVELSL
DVSEKTG
//
