ID B8HD80_PSECP Unreviewed; 387 AA.
AC B8HD80;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:ACL40726.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:ACL40726.1};
GN OrderedLocusNames=Achl_2761 {ECO:0000313|EMBL:ACL40726.1};
OS Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS chlorophenolicus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudarthrobacter.
OX NCBI_TaxID=452863 {ECO:0000313|EMBL:ACL40726.1, ECO:0000313|Proteomes:UP000002505};
RN [1] {ECO:0000313|EMBL:ACL40726.1, ECO:0000313|Proteomes:UP000002505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 /
RC NCIMB 13794 / A6 {ECO:0000313|Proteomes:UP000002505};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL Submitted (JAN-2009) 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}.
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DR EMBL; CP001341; ACL40726.1; -; Genomic_DNA.
DR RefSeq; WP_015937922.1; NC_011886.1.
DR AlphaFoldDB; B8HD80; -.
DR STRING; 452863.Achl_2761; -.
DR KEGG; ach:Achl_2761; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_11; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000002505; Chromosome.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF92; 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 Transferase {ECO:0000313|EMBL:ACL40726.1}.
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 387 AA; 41042 MW; 2F2D1503A03B57C0 CRC64;
MSLQENQGFN TRAVHAGQAF EPRTGAVVPP LHFSSTYAQD GIGNLRSGYE YGRGGNPTRD
ALQEQLAALE LGTHAYSFSS GLAAEDALIR ALTRPGDHIV LGNDAYGGTY RLISRVLGDW
GIGNTPVDMA NLDTVRRAVA ANKTRFVWVE TPSNPLMKIT DIAALADIAH DAGALLVVDN
TFASPYLQNP LALGADVVVH STTKYIGGHS DVVGGAVVVK DAELADKIGF VQFAVGAVSG
PMDAFLTTRG LKTLGVRMDR HSENGQAVAE WLLERPEVEA VLYPGLPSHP GHELAKSQMR
SFGGMVSVQF KGGEAAARKV AESTSVFTLA ESLGGIESLM NYPSEMTHAS VKGTELAVPV
NLLRLSCGIE DKEDLVADLE QAFSSIP
//
