ID I3ZA62_BELBD Unreviewed; 382 AA.
AC I3ZA62;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Cystathionine beta-lyase/cystathionine gamma-synthase {ECO:0000313|EMBL:AFL86130.1};
DE EC=4.4.1.1 {ECO:0000313|EMBL:AFL86130.1};
GN OrderedLocusNames=Belba_3638 {ECO:0000313|EMBL:AFL86130.1};
OS Belliella baltica (strain DSM 15883 / CIP 108006 / LMG 21964 / BA134).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Belliella.
OX NCBI_TaxID=866536 {ECO:0000313|EMBL:AFL86130.1, ECO:0000313|Proteomes:UP000006050};
RN [1] {ECO:0000313|Proteomes:UP000006050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15883 / CIP 108006 / LMG 21964 / BA134
RC {ECO:0000313|Proteomes:UP000006050};
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Mikhailova N., Davenport K., Kyrpides N., Mavromatis K., Pagani I.,
RA Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Belliella baltica DSM 15883.";
RL Submitted (JUN-2012) 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; CP003281; AFL86130.1; -; Genomic_DNA.
DR RefSeq; WP_014774064.1; NC_018010.1.
DR AlphaFoldDB; I3ZA62; -.
DR STRING; 866536.Belba_3638; -.
DR KEGG; bbd:Belba_3638; -.
DR PATRIC; fig|866536.3.peg.3766; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_10; -.
DR OrthoDB; 634606at2; -.
DR Proteomes; UP000006050; Chromosome.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR GO; GO:0044540; F:L-cystine L-cysteine-lyase (deaminating); 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:AFL86130.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006050}.
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 382 AA; 42193 MW; 29B07A9C6DD51558 CRC64;
MKFGTKAIHA GVEPDPSTGA IMTPIYQTST YVQRSPGDHQ GYEYSRTHNP TRTALQNNLA
ALENGKHGLC FSSGLGAIDA IIKLLNPGDE VISTNDLYGG SYRIFTKVFE RYGIKFHFVS
MENPESIEKY VNDRTKLIWA ETPTNPMMNI IDVAGIATVA KKHHVLFAVD NTFATPFLQN
PLDLGADIVM HSVTKYLGGH SDVVMGAIIV NDDHLADQLA FIQNACGATP GPQDCFLVLR
GIKTLHIRME RHCQNGKTIA AYLKNHPKVE KVYWPGFEDH PNHQIAKKQM RDFGGMISFT
LKGNKIEDAK KILENLHFFA LAESLGGVES LCGHPASMTH ASIPKEEREK IGLVDSLIRL
SVGIEDAEDL KEDLKKALDI IS
//
