ID A0A0Q3WVZ4_9BACI Unreviewed; 379 AA.
AC A0A0Q3WVZ4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:KQL53028.1};
GN ORFNames=AN964_05545 {ECO:0000313|EMBL:KQL53028.1};
OS Heyndrickxia shackletonii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=157838 {ECO:0000313|EMBL:KQL53028.1, ECO:0000313|Proteomes:UP000051888};
RN [1] {ECO:0000313|EMBL:KQL53028.1, ECO:0000313|Proteomes:UP000051888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 18435 {ECO:0000313|EMBL:KQL53028.1,
RC ECO:0000313|Proteomes:UP000051888};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (SEP-2015) 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:KQL53028.1}.
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; LJJC01000004; KQL53028.1; -; Genomic_DNA.
DR RefSeq; WP_055738743.1; NZ_LJJC01000004.1.
DR AlphaFoldDB; A0A0Q3WVZ4; -.
DR STRING; 157838.AN964_05545; -.
DR PATRIC; fig|157838.3.peg.1233; -.
DR OrthoDB; 9803887at2; -.
DR Proteomes; UP000051888; 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:SF90; CYSTATHIONINE GAMMA-LYASE; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000051888}.
FT MOD_RES 205
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 379 AA; 41034 MW; 1F108063DABF7D7B CRC64;
MDVSFDTKVV HNSLKNTNSI HSKTTPIYQT TAFTFSSLEE LEGFYQGKSP YLYSRTGNPN
TDELGQAVAA LEGAPAGVAT SSGLSAILAG ILSVAKAGDH VVAAEDLYGG TYHLLKEELK
QFGIETTFVP FENSAQVKNA IQKNTTLLYT ETVTNPFLRV ENIGKLVEIA KEKSIITMVD
NTFASPYLKQ PYLEGVNLVV HSATKYLGGH SDVTAGVLVG HTDIVKKARE KVVNLGANLS
PFEAWLACRG LKTLALRMER QALNAKELAH ALNANPSVKK VYYPEYVSEK GNGAIVTIEL
GENCDISRFF SSLGWVKIVP TLAGVETTVS YPLGTSHRAL PPELQDKIGI NKQVVRISIG
IESASDIIKQ FEQAIQASL
//
