ID A0A1W6YI35_9BORD Unreviewed; 766 AA.
AC A0A1W6YI35;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C {ECO:0000313|EMBL:ARP80701.1};
GN ORFNames=CAL12_07510 {ECO:0000313|EMBL:ARP80701.1};
OS Bordetella genomosp. 8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1416806 {ECO:0000313|EMBL:ARP80701.1, ECO:0000313|Proteomes:UP000194151};
RN [1] {ECO:0000313|EMBL:ARP80701.1, ECO:0000313|Proteomes:UP000194151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU19157 {ECO:0000313|EMBL:ARP80701.1,
RC ECO:0000313|Proteomes:UP000194151};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) 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; CP021108; ARP80701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6YI35; -.
DR STRING; 1416806.CAL12_07510; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000194151; Chromosome.
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:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR CDD; cd02769; MopB_DMSOR-BSOR-TMAOR; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.90.55.10; Dimethylsulfoxide Reductase, domain 3; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041954; CT_DMSOR/BSOR/TMAOR.
DR InterPro; IPR041460; Molybdopterin_N.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR PANTHER; PTHR43742:SF10; TRIMETHYLAMINE-N-OXIDE REDUCTASE 2; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF18364; Molybdopterin_N; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000313|EMBL:ARP80701.1}.
FT DOMAIN 14..53
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 57..514
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 631..749
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 766 AA; 83905 MW; FDA5628B1FBF8F3F CRC64;
MTSIPSHERR YPQLAHWGAF NAVVRDGRLV ACEPFEQDPA PSRMLEAIAP MVYSPRRIAR
PAVRKSWLAT HGAAGGELRG RDEFVEVDWD VALDLVAAEI GRTREEQGAD GIFCGSYGWS
SAGRLHHARS LIRRFYFAGG GGVDQVGNYS WGTAQFILPH VIGTYTPLTG RVTSWPSIIA
HTDVFLAFGG LALKNGQVSS GGAAEHTQEY WLRQLAAKGA RVVNVSPTRG DCPAFLDAEW
IPIRPNTDVA LMLALAHELR RMDAHDPAFL ASHCVGYPAL EAYFMGTADG VPKSPEWAAP
ITGIPAERIR ELARALRGTR SYLTCSFAVQ RAQHGEQPYW MAIALAAMLG QIGLPGGGFG
FGHGSMNGVG NPRIATPGPE MPVGRNPADL SIPVARLTDM LERPGQPYPF QGQTHRYPDI
HFIHWAGGNP FHHHQQLNRL LRAWRDKPRT IVVNEIWWTP VARHADIVLP ITTSLERNDI
GGSSRDRYAL AMHRAIDPVG QARNDLDVFA DLAQRLGYRD RYTEGRDEMA WIRHIYAQFA
RTQEHAGITM PDFDAFWRLG HVRLPSPATD FILFEDFRED PAAHPLRTPS GRIELYSQTL
ASYGCEDCGP HPRWMPPGEW LGAPAARDYP LHLLTVQPAD RLHSQLDPAP LAQSGKVAGR
EAVRIHPADA QARGLRDGDV VRLYNARGAC LAGARLDDGL LPGTVVMATG AWFAPPAGDD
APEDAGTANV LTLDVGTSTL TQGPNAMSCL VQAERWRAGR NDTTGA
//
