ID F9RLN2_9VIBR Unreviewed; 422 AA.
AC F9RLN2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Putative homocysteine synthase {ECO:0000313|EMBL:EGU39036.1};
GN ORFNames=VIS19158_05693 {ECO:0000313|EMBL:EGU39036.1};
OS Vibrio scophthalmi LMG 19158.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=870967 {ECO:0000313|EMBL:EGU39036.1, ECO:0000313|Proteomes:UP000004349};
RN [1] {ECO:0000313|EMBL:EGU39036.1, ECO:0000313|Proteomes:UP000004349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 19158 {ECO:0000313|EMBL:EGU39036.1,
RC ECO:0000313|Proteomes:UP000004349};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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:EGU39036.1}.
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DR EMBL; AFWE01000073; EGU39036.1; -; Genomic_DNA.
DR RefSeq; WP_005594235.1; NZ_AFWE01000073.1.
DR AlphaFoldDB; F9RLN2; -.
DR eggNOG; COG2873; Bacteria.
DR Proteomes; UP000004349; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01326; OAH_OAS_sulfhy; 1.
DR PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR PANTHER; PTHR43797:SF2; HOMOCYSTEINE_CYSTEINE SYNTHASE; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 422 AA; 45775 MW; 87074EC0B009F50D CRC64;
MKDETLAIHF GYETEPTTKS VATPIYQTVA YEFDSAQHGA DLFNLEVPGN IYTRIMNPTN
DVLEKRIAAL EGGIAGLVVS AGSAAINYAI LTLAEAGDNI VSTPQLYGGT YTLFAHMLPK
QGIEVRFAKD DKPESLAELI DENTKAVYCE SIGNPAGNII DLERVAAVAH AQGVPVIVDN
TVATPALCKP IEFGADIVVH SLTKYVGGHG TTLGGAIIDA GTFPWAEHKE RFPVMNQPEP
SYHGVVYTEA FGPAAFIGRA RTVPLRNTGA ALSPMNAFML MQGLETLSLR MERHTENALK
VAQYLQQHEK VSWVSYAGLA DSPFYPLAEK YMQGKPSAIL SFGLKDGYDA GVRFYDALQI
FKRLVNIGDA KSLACHPAST THRQMSTEEQ AKAGVYPEMI RLSVGIEHID DILDDLDQAL
RA
//
