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Database: UniProt
Entry: H0Q4M3_9RHOO
LinkDB: H0Q4M3_9RHOO
Original site: H0Q4M3_9RHOO 
ID   H0Q4M3_9RHOO            Unreviewed;       879 AA.
AC   H0Q4M3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:BAL26936.1};
GN   ORFNames=AZKH_p0053 {ECO:0000313|EMBL:BAL26936.1};
OS   Azoarcus sp. KH32C.
OG   Plasmid pAZKH {ECO:0000313|EMBL:BAL26936.1,
OG   ECO:0000313|Proteomes:UP000007106}.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=748247 {ECO:0000313|EMBL:BAL26936.1, ECO:0000313|Proteomes:UP000007106};
RN   [1] {ECO:0000313|EMBL:BAL26936.1, ECO:0000313|Proteomes:UP000007106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH32C {ECO:0000313|EMBL:BAL26936.1,
RC   ECO:0000313|Proteomes:UP000007106};
RC   PLASMID=Plasmid pAZKH {ECO:0000313|Proteomes:UP000007106};
RA   Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S.,
RA   Senoo K.;
RT   "Complete genome sequence of Azoarcus sp. KH32C.";
RL   Submitted (NOV-2011) 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   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; AP012305; BAL26936.1; -; Genomic_DNA.
DR   RefSeq; WP_015451713.1; NC_020548.1.
DR   AlphaFoldDB; H0Q4M3; -.
DR   KEGG; aza:AZKH_p0053; -.
DR   PATRIC; fig|748247.4.peg.4625; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_9_0_4; -.
DR   OrthoDB; 9815647at2; -.
DR   Proteomes; UP000007106; Plasmid pAZKH.
DR   GO; GO:0051536; F:iron-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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02780; MopB_CT_Tetrathionate_Arsenate-R; 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; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037946; MopB_CT_Tetrathionate.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR   PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   Pfam; PF10518; TAT_signal; 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; PS51318; TAT; 1.
PE   3: Inferred from homology;
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Plasmid {ECO:0000313|EMBL:BAL26936.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007106};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          48..105
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   879 AA;  98502 MW;  1E7BBC2232818C48 CRC64;
     MEFPKITRRT FLKASAGTTA AAATAPRLLH AMENELGGKD FDPVNAAERK AIPINCHVCN
     IQDGAIAYVE NDRVVKLEGN PEHVSTRGRL CAKGNSGMWY SYDPDRILYP LKRVGARGEG
     KWKRITWDEA LAEVAQKLDA ALKEDPNTIM MKYGRNRTGG TLDRFMQTLG SATVVNHTSV
     CESSKKVGME PTWGPDIETP DFANAKYVLN FGSNVLEAAY FHNPLSQRVT EGRIDNQMKI
     VTFDVRLSNT AGFSDEWIPV FPATDGAVAL SIGHVILRED LQDSDFINTW TNVTVDELKA
     HYAQYTPEWA SKISGVPVAT IERIAREFAT TKPATLFTYR GPAKHLYGSY NEKACMMLPI
     MTGNVEKRGG YCLPRGMGWP QPEPQPGKPV KASYLAHPPD YPLAAHKVSH LVPFWIAEGK
     QKINVYFTYQ DNPVYTNPGS MAVWGKLYKD EKLIPYFVSM SPFMGEETAL ADLILPDCPY
     LERWEPESMP NSLWPWLGIR QPVHKSLGES RENRVMLRDI IWKLDPDGSR GMKKFWDFKD
     GEDYMRHHFD NVPGLKEAGG LDFLKKHGVW PIYGKLDPRT GKVTDKTGRE IQAEYGLYRK
     ELSAADMEGA MVDARGLITK NGKAIGIRRN GKNHVGFPTG NRLINVRVDE WAEYGFNPMP
     TFKRIPWHET MSDDEMILST FKLNVHKQSR TAAVKWLAEI AHSNPAWMNP ETAKKLGVKT
     GDLVRIESAV GYLVTKAYVT EGIHPKVVSI PTGFGHWEYG RLATLRLKDK KGDASHGQDD
     PDLNNVWWDD RGVHPNNIIP VVADPIGGSQ GWFDTVVKVT KAGPNDKYGD TQGDWDKHVA
     AFKETMRYAY TGDLHRKMHP EMAAWAGPDS VKKKAPGGH
//
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