GenomeNet

Database: UniProt
Entry: Q7V8V0_PROMM
LinkDB: Q7V8V0_PROMM
Original site: Q7V8V0_PROMM 
ID   Q7V8V0_PROMM            Unreviewed;       490 AA.
AC   Q7V8V0;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=Possible cystathionine gamma-synthase {ECO:0000313|EMBL:CAE20400.1};
GN   OrderedLocusNames=PMT_0225 {ECO:0000313|EMBL:CAE20400.1};
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=74547 {ECO:0000313|EMBL:CAE20400.1, ECO:0000313|Proteomes:UP000001423};
RN   [1] {ECO:0000313|EMBL:CAE20400.1, ECO:0000313|Proteomes:UP000001423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313 {ECO:0000313|Proteomes:UP000001423};
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
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|RuleBase:RU362118}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX548175; CAE20400.1; -; Genomic_DNA.
DR   RefSeq; WP_011129604.1; NC_005071.1.
DR   AlphaFoldDB; Q7V8V0; -.
DR   KEGG; pmt:PMT_0225; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_011302_2_0_3; -.
DR   OrthoDB; 262490at2; -.
DR   Proteomes; UP000001423; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42699; -; 1.
DR   PANTHER; PTHR42699:SF1; CYSTATHIONINE GAMMA-SYNTHASE-RELATED; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU362118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001423}.
SQ   SEQUENCE   490 AA;  52729 MW;  7DDDF3B8515679BF CRC64;
     MSPRDLLQDP CWHADELGKA LPDSPHAVSV ALPRWQDVVA YEEKDPACLK ALQAIYPRFG
     FHPLVAEIAQ KARKEHGCAD DGSAWPYPTA AAAERARFHC QRSEPMAKTS IKTVLGLPCL
     LTDAKGCSAA KAFWQHSGLG ASSRQAASAL GQEPFPSLQA SAAAQTLLKQ RLAEIYGCDP
     ELVQLHPSGM AALTKALQAI TALRPGKPCL QLGFPYVDVL KLPEVVFGGC DLLLTTDLNR
     LALELDRRQP AAVIVELPSN PMLQCVDLPA VARLAKARGI PVIADDTIGS PLNLDALPHA
     DLVFSSLTKS FAGRGDILAG SLVVSPSSPW REELSRELST ALAPLGDADA IALEQASRDV
     AQRLPQLNNA CQRLADKLAC HPSIARVHHP GQCTNFQALM RPGAGHGCLL SFELWGGIEQ
     AKRVYDALQV CKGPSLGTSF TLVCPYVLLA HYNELSWAES CGVPSHLLRV SVGLEDPDNL
     WRRFEMALKA
//
DBGET integrated database retrieval system