ID Q9CMT7_PASMU Unreviewed; 1029 AA.
AC Q9CMT7;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE SubName: Full=TtrA {ECO:0000313|EMBL:AAK02805.1};
GN Name=ttrA {ECO:0000313|EMBL:AAK02805.1};
GN OrderedLocusNames=PM0721 {ECO:0000313|EMBL:AAK02805.1};
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843 {ECO:0000313|EMBL:AAK02805.1, ECO:0000313|Proteomes:UP000000809};
RN [1] {ECO:0000313|EMBL:AAK02805.1, ECO:0000313|Proteomes:UP000000809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70 {ECO:0000313|EMBL:AAK02805.1,
RC ECO:0000313|Proteomes:UP000000809};
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02805.1; -; Genomic_DNA.
DR RefSeq; WP_010906816.1; NC_002663.1.
DR AlphaFoldDB; Q9CMT7; -.
DR STRING; 272843.PM0721; -.
DR EnsemblBacteria; AAK02805; AAK02805; PM0721.
DR KEGG; pmu:PM0721; -.
DR PATRIC; fig|272843.6.peg.729; -.
DR HOGENOM; CLU_008235_0_0_6; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000000809; Chromosome.
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 CDD; cd02758; MopB_Tetrathionate-Ra; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 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; IPR041929; Tetrathionate-R_A_N.
DR PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000000809};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 71..155
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1029 AA; 113143 MW; 883FA2918615A600 CRC64;
MNNQRRNLLK GGLALGTATA FVTGYSPKVK EIATGLLEGT SGEHTQDKIN GNALTPEYQV
QQGKLISNSH QVVCNTQCMG CWTLCGLRAR VDLAKNQVLR INGNPYHPLS ADQYLDFNQP
IQQAELSVAG ESGLANRSTA CARGAAFLEG INSPYRLTQP LKRVGKRGEG KWQTISFEQL
VDEVVNGGDL FGEGHVEGLK TIRDLQTPVD QENPEFGAKV NQLMVTFAGP EGRQPLLKRF
ANNSFGTINF ASHGSFCGLS YRAGSGAFMN DLANNAHAKP DWDHAEFILF MGTSPAQAGN
PFKRQARQLA KQRTEDNFDY VVVAPRLELS SSRAVNQHRW VPIVPGTDLS LSLAMLRWII
ENARYNADYL AIPSENAMQS ANAVSFCNAT HLFIADPQHK RYGQALRVQD VMDSPTPEKP
EDGDILVKDQ QTGAMIAAKD SQSAVLFVEE MVTLKEGTSV LAKSALQLFK ESCFEHSIEQ
YSAHCGVPVA TIIELAKKFT SHGHRAAVVT HGGTMHGTGF YTAWAILLLN AMVGNMNKKG
GMSMSGGKFK DFGAGPRYDL ANFPNMVNPK GTNLARSKRA YEKSSEFKRK VEQGLSPYPA
KASWYPFVGG QMSEMITSAL QGYPYPLKAW ISHMSNPIYG MTGIHHITDE KLRDPRILPL
FIAVDAFMNE TTALADYIVP DTHNFESWGF STPWAGVPTK TSTARWPIIQ SHNAKTASGE
TICMESFIIA IAKAMDLPGF GENAISDKQK NSYPLNCTED YFLRAAANIA YDGKTPVNDA
TEEDLLLTGV QRLMPTLQRT LKAEEVLKVA NVYCKGGRFA PYKSAWQEEN MQARWKNCLQ
IWNETVAKAK HAQTGQHYHG CPKYFEPQFA DNSTLESHYP SKEWPFKLIS FKSNLMSSIT
APLLRLQSIK PEGIVAMNQQ DAQTQGLRHG DLVELSTPGG KGLVQIIVME GVIKGTIAIE
HGYGHKQLGA TSYVIDGKEI QGAPQIQRGI NINDLGLLDN TKEIVSPWVD WVCGSAVRQG
IPAKLQKVI
//
