ID A0A2A3K0A8_9RHOB Unreviewed; 527 AA.
AC A0A2A3K0A8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Alanine-phosphoribitol ligase {ECO:0000313|EMBL:PBD20866.1};
GN ORFNames=CLG85_01415 {ECO:0000313|EMBL:PBD20866.1};
OS Alloyangia mangrovi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Alloyangia.
OX NCBI_TaxID=1779329 {ECO:0000313|EMBL:PBD20866.1};
RN [1] {ECO:0000313|EMBL:PBD20866.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAOS 153D {ECO:0000313|EMBL:PBD20866.1};
RA Verma A., Krishnamurthi S.;
RT "Yangia sp. SAOS 153D whole genome sequencing.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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:PBD20866.1}.
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DR EMBL; NTHN01000018; PBD20866.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3K0A8; -.
DR OrthoDB; 9785276at2; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968}; Ligase {ECO:0000313|EMBL:PBD20866.1}.
FT DOMAIN 81..104
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 253..267
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 83
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 527 AA; 57374 MW; 8F9AD7D2ED8D641D CRC64;
MQSVDYVIVG GGSTGCVVAS RLSENQSCEV ALLEEGPRDR NPYIHIPGAY YKTAQGPLLK
RYEWEARPEQ QRPERETMVQ ARVLGGGSSV NAMIYIRGNP QDYDGWASAG AEGWSYEDVL
PYFRKSESNN RFAGETHGTD GPLKVSDIDS IHPLTRAWLQ ACQQQGLPFN PDFNSGTQAG
TGLYQITSRG RRRSSAAVAY LHPALARRNL QVKTGAQVTR VIVENGRATG VEFLQGGKRR
VLMAREEVIL SAGAVATPHL MMRSGLGPAD VLQRHGIAVQ QDLPGVGQNL QDHIEISLVY
QLNGPHSYDR YKKLHWKALA GLEYLMFGKG PAVSNLIEGG AFWWGDKSEA LPDCQFFLVC
GAGIEEGVDG VPGGNGCTVN LGQVRPYSRG EVTLRSGDSE AAPIIRPNYF GDPRDLEAVT
DATLFAMDVM EQPAISRFVE RRHVPDATRS TRDSIRQFCQ REAHAALHPC GTARIGKDNM
AVVDPSLRVH GVDGLRVADA SVMPNIVSGN LNAVCMMIGE KAADLMS
//
