ID A0A261SNK7_9BORD Unreviewed; 778 AA.
AC A0A261SNK7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C {ECO:0000313|EMBL:OZI38627.1};
GN ORFNames=CAL29_05170 {ECO:0000313|EMBL:OZI38627.1};
OS Bordetella genomosp. 10.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1416804 {ECO:0000313|EMBL:OZI38627.1, ECO:0000313|Proteomes:UP000216020};
RN [1] {ECO:0000313|EMBL:OZI38627.1, ECO:0000313|Proteomes:UP000216020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU16122 {ECO:0000313|EMBL:OZI38627.1,
RC ECO:0000313|Proteomes:UP000216020};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZI38627.1}.
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DR EMBL; NEVM01000001; OZI38627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261SNK7; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000216020; Unassembled WGS sequence.
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 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 InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
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.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000313|EMBL:OZI38627.1}.
FT DOMAIN 9..49
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 53..505
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 626..740
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT REGION 747..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 85784 MW; B9F950EC6CA9A3A7 CRC64;
MSAVTRHPTL SHWGAYTALV QDGRLIACEP FPHDPAPSSL IHAMPAMVHS PLRVRRPAVR
EGWLRNRDTA GRGSDRYVET SWDQALRLVH EELQRVRAEH GPHGVFGGSY GWASAGRVHS
AITQTHRFLY AGGGCVEQAG NYSWGAAQFL LPHVIGTYKP LTGRVTDWNS VSRHTDLLLA
FGGMPLRNAQ MIAGGAGAHT TEHWLRRTAE RGARFVIVSP TRGDVPPWLD AEWIPIRPNT
DVAMMIAMAH TLLAESRHDA AFLHTHCEGY AAYAAYLRGD GDGQPKDAEW AQAICGVPAA
TIRGLARNAA GCRTLINCTW SLQRAHRGEQ PYWASIALAA ILGQIGLPGG GFSFGTGSIN
SASNPRPDVA GPEMPELRNP APRNIPVARI ADMLLAPGAE YQFNGRTGIY PDVRLVYWAG
GNPFHHHQDL NRLARAWRKP ETIVVHESWW TPTARRADIV LPATTTLERN DIGGSTRDRY
VFAMHQALPP QGESRSDFDI YRELAALGGF EAAFTEGRGE MDWIRHVYAR MGERWRKGPI
PMPSPPPFEA FWERGYLELP ESERDFILFE DFRRDPAAHP LQTPSGRIEL YSSKVAGFGY
EDCPPHPCWL PPAEWLGAPA AQRWPLHLIT SQPADRLHSQ LDPAPQSRRH KIQGREPIRI
HPDDAARRGI KDGMLVRVFN ARGACLAGAM LDIGVSPGVL VMSTGAWFDP GKELERHGNP
NVLTLDIGTS QLTQGTSAQS ALVEIEPWTG PAPEMRAYES PLARDAGDED GQTPISRE
//