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Database: UniProt
Entry: V2UCH9_9GAMM
LinkDB: V2UCH9_9GAMM
Original site: V2UCH9_9GAMM 
ID   V2UCH9_9GAMM            Unreviewed;       394 AA.
AC   V2UCH9;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Cystathionine beta-lyase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=P255_00300 {ECO:0000313|EMBL:ESK52158.1};
OS   Acinetobacter brisouii CIP 110357.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1341683 {ECO:0000313|EMBL:ESK52158.1, ECO:0000313|Proteomes:UP000018418};
RN   [1] {ECO:0000313|EMBL:ESK52158.1, ECO:0000313|Proteomes:UP000018418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 110357 {ECO:0000313|EMBL:ESK52158.1,
RC   ECO:0000313|Proteomes:UP000018418};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA   Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter brisouii CIP 110357.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate;
CC         Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199;
CC         Evidence={ECO:0000256|ARBA:ARBA00001535};
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}.
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:ESK52158.1}.
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DR   EMBL; AYEU01000003; ESK52158.1; -; Genomic_DNA.
DR   RefSeq; WP_004899348.1; NZ_KI530762.1.
DR   AlphaFoldDB; V2UCH9; -.
DR   STRING; 396323.VH98_00320; -.
DR   PATRIC; fig|1341683.3.peg.294; -.
DR   HOGENOM; CLU_018986_5_1_6; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000018418; Unassembled WGS sequence.
DR   GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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; IPR006233; Cys_b_lyase_bac.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43500; CYSTATHIONINE BETA-LYASE-RELATED; 1.
DR   PANTHER; PTHR43500:SF1; CYSTATHIONINE BETA-LYASE-RELATED; 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:UP000018418}.
FT   MOD_RES         209
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   394 AA;  44245 MW;  CC6564834F8A7EF5 CRC64;
     MKKSSQTELI HAPRLAPQYI KTIQPPLYRA STIIFENTSK LFDRHWSDRY DYSYGTHGTP
     TTYTLADKIA QLENGNYCLL APSGLSAINL VNSALLQSGD EVWVPDNIYG PGMAHLRYLQ
     QSFGVIVQVY DPLDHHSFQP STKAKLVWLE AAGSVTLEFP DLINLVKKAK QHQIMTVLDN
     TWGAGLAFNA FDFSDEHLAV DITVHALTKY PSGGGDILMG SVVTQEHKLH LKLLHMHATQ
     GIAVSGDDCA QIQRSLAHMQ LRYQQQSHSA QEILHWLKQQ PQFQQVLHPS DALSPGHQYW
     QQVCQSQQSA GLVSVIFQEN YTLESIRRFC DALQLFKLGF SWGGPVSLVM LYDLTEMRSL
     KSAHLAQGFL VRFCIGLESS EDLIRDIEQA LQAL
//
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