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Database: UniProt
Entry: A6D4U9_9VIBR
LinkDB: A6D4U9_9VIBR
Original site: A6D4U9_9VIBR 
ID   A6D4U9_9VIBR            Unreviewed;       422 AA.
AC   A6D4U9;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Homocysteine synthase {ECO:0000313|EMBL:EDL52389.1};
GN   ORFNames=VSAK1_14570 {ECO:0000313|EMBL:EDL52389.1};
OS   Vibrio mediterranei AK1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=391591 {ECO:0000313|EMBL:EDL52389.1, ECO:0000313|Proteomes:UP000003769};
RN   [1] {ECO:0000313|EMBL:EDL52389.1, ECO:0000313|Proteomes:UP000003769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK1 {ECO:0000313|EMBL:EDL52389.1,
RC   ECO:0000313|Proteomes:UP000003769};
RA   Rosenberg E., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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:EDL52389.1}.
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DR   EMBL; ABCH01000033; EDL52389.1; -; Genomic_DNA.
DR   RefSeq; WP_006073626.1; NZ_ABCH01000033.1.
DR   AlphaFoldDB; A6D4U9; -.
DR   GeneID; 64088821; -.
DR   Proteomes; UP000003769; 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;  45909 MW;  3D0E6C74E0685E16 CRC64;
     MKDETLSIHH GYETDPTTKS VATPIYQTVA YEFDSAQHGA DLFNLEVPGN IYTRIMNPTN
     DVLEQRMAAL EGGIAGLVVS AGSAAINYAI LTLAEAGDNI VSTPQLYGGT YTLFAHMLPK
     QGIQVKFAKD DKPESIAELI DENTKAVYCE SIGNPAGNIV DLEGISSLAH QQGVPVIVDN
     TVATPILCKP IEHGADIVVH SLTKYVGGHG TSLGGVIIDS GKFPWDQHKE RFPVFNQPEP
     SYHGVVYTEA FGPAAFIGRA RTVPLRNTGS ALSPMNAFML LQGLETLPLR MERHTENALK
     VAQYLQQHEK VSWVSYAGLE DSAHYELACK YMDGKPSAIL SFGLKDGYEA GVRFYDALQI
     FKRLVNIGDA KSLACHPAST THRQMSESEQ LEAGVRPEMI RLSVGIEHID DILADLEQAL
     KA
//
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