ID A0A097R7L4_HAFAL Unreviewed; 387 AA.
AC A0A097R7L4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:AIU74718.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:AIU74718.1};
GN ORFNames=AT03_00030 {ECO:0000313|EMBL:AIU70946.1}, AT03_21450
GN {ECO:0000313|EMBL:AIU74718.1};
OS Hafnia alvei FB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU74718.1, ECO:0000313|Proteomes:UP000029986};
RN [1] {ECO:0000313|EMBL:AIU74718.1, ECO:0000313|Proteomes:UP000029986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB1 {ECO:0000313|EMBL:AIU74718.1,
RC ECO:0000313|Proteomes:UP000029986};
RX PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA Tan J.Y., Yin W.F., Chan K.G.;
RT "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT pathogenesis: a draft genome perspective.";
RL Gut Pathog. 6:29-29(2014).
RN [2] {ECO:0000313|EMBL:AIU74718.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FB1 {ECO:0000313|EMBL:AIU74718.1};
RA Tan J.-Y., Chan K.-G.;
RT "Complete genome of Hafnia alvei FB1.";
RL Submitted (OCT-2014) 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|RuleBase:RU362118}.
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DR EMBL; CP009706; AIU70946.1; -; Genomic_DNA.
DR EMBL; CP009706; AIU74718.1; -; Genomic_DNA.
DR RefSeq; WP_025799614.1; NZ_CP009706.1.
DR AlphaFoldDB; A0A097R7L4; -.
DR KEGG; hav:AT03_00030; -.
DR KEGG; hav:AT03_21450; -.
DR PATRIC; fig|1453496.5.peg.11; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_6; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000029986; Chromosome.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; 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; IPR011821; O_succ_thio_ly.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR02080; O_succ_thio_ly; 1.
DR PANTHER; PTHR11808:SF75; CYSTATHIONINE GAMMA-SYNTHASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000029986};
KW Transferase {ECO:0000313|EMBL:AIU74718.1}.
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 387 AA; 41771 MW; 9B6352970137002F CRC64;
MTYKQATLAV RSGLNDDEQY GCVVPPIHLS STYNFTDFNE PRAHDYSRRG NPTRDVVQRA
LAELEGGAGA VMTSTGMSAI HLVCTVFLKP GDLLVAPHDC YGGSYRLFDS LAKRGAYNVL
FVDQGDAQAL AAALEQKPKL VLIETPSNPL LRVVDIAAIC TAAKAVGALT VVDNTFLSPA
LQQPLKLGAD LVLHSCTKYL NGHSDVVAGT VIAKDPAHVT ELAWWANNIG VTGSAFDSYL
LLRGLRTLSP RIQLQQQNAL KIVEFLKHQP LVKKLYHPSL PENPGHEIAC RQQSGFGAML
SFELDGDEAL LRRFLKSLQL FTLAESLGGV ESLISHAGTM THAGMAPEAR KAAGISESLL
RISVGIEDGD DLISDLEQAF QKANSQR
//
