ID U2KGE7_9STRE Unreviewed; 364 AA.
AC U2KGE7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:ERJ76239.1};
GN ORFNames=HMPREF1557_01133 {ECO:0000313|EMBL:ERJ76239.1};
OS Streptococcus sobrinus W1703.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1227275 {ECO:0000313|EMBL:ERJ76239.1, ECO:0000313|Proteomes:UP000016617};
RN [1] {ECO:0000313|EMBL:ERJ76239.1, ECO:0000313|Proteomes:UP000016617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W1703 {ECO:0000313|EMBL:ERJ76239.1,
RC ECO:0000313|Proteomes:UP000016617};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-2013) 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}.
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:ERJ76239.1}.
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DR EMBL; AWVA01000069; ERJ76239.1; -; Genomic_DNA.
DR RefSeq; WP_002960340.1; NZ_KI259683.1.
DR AlphaFoldDB; U2KGE7; -.
DR PATRIC; fig|1227275.3.peg.1002; -.
DR HOGENOM; CLU_018986_2_0_9; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000016617; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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:SF91; 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}.
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 364 AA; 39714 MW; 1EAB46B92BF79AFF CRC64;
MTQDYKLATI LAHAGINSDK ETGALAAPLH FSTTYQHPEF GQSTGFDYTR TKNPTRATLE
KTLAAIEKAD YAIATSSGMS AIVLALEIFP VGSKVVAARD LYGGSFRWFN DQEEQGRFSF
TYANSQAEMV AAISDDTDIV YIETPTNPLM IEFDIKTVAE LAHQKGAVVI VDNTFYSPIY
QNPIELGADI VVHSATKYLA GHNDVLAGVV ITSNQDYYDK LLYNLNTTGP NLSPFDSYML
MRGLKTLKLR MEASTKNAQS VANFLQESPA VKEVLYTGKG GMVSFKVKDQ AKIPAIINSL
QVFTFAESLG GVESLITYPT TQTHADIPAA VRASYGLTDD LLRLSIGIED SQDLVNDLKQ
ALES
//
