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Database: UniProt
Entry: F0P2M2_WEEVC
LinkDB: F0P2M2_WEEVC
Original site: F0P2M2_WEEVC 
ID   F0P2M2_WEEVC            Unreviewed;       383 AA.
AC   F0P2M2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:ADX67861.1};
DE            EC=4.4.1.1 {ECO:0000313|EMBL:ADX67861.1};
GN   OrderedLocusNames=Weevi_1152 {ECO:0000313|EMBL:ADX67861.1};
OS   Weeksella virosa (strain ATCC 43766 / DSM 16922 / JCM 21250 / CCUG 30538 /
OS   CDC 9751 / IAM 14551 / NBRC 16016 / NCTC 11634 / CL345/78).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Weeksella.
OX   NCBI_TaxID=865938 {ECO:0000313|EMBL:ADX67861.1, ECO:0000313|Proteomes:UP000008641};
RN   [1] {ECO:0000313|EMBL:ADX67861.1, ECO:0000313|Proteomes:UP000008641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43766 / DSM 16922 / JCM 21250 / NBRC 16016 / NCTC 11634 /
RC   CL345/78 {ECO:0000313|Proteomes:UP000008641};
RX   PubMed=21475590;
RA   Lang E., Teshima H., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA   Nolan M., Cheng J.F., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA   Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brambilla E.M., Kopitz M., Rohde M., Goker M., Tindall B.J., Detter J.C.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Weeksella virosa type strain (9751).";
RL   Stand. Genomic Sci. 4:81-90(2011).
RN   [2] {ECO:0000313|Proteomes:UP000008641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43766 / DSM 16922 / JCM 21250 / NBRC 16016 / NCTC 11634 /
RC   CL345/78 {ECO:0000313|Proteomes:UP000008641};
RX   DOI=10.4056/sigs.1603927;
RA   Lang E., Teshima H., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA   Nolan M., Cheng J., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA   Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Brambilla E.,
RA   Kopitz M., Rohde M., Goker M., Tindall B., Detter J., Woyke T., Bristow J.,
RA   Eisen J., Markowitz V., Hugenholtz P., Klenk H., Kyrpides N.;
RT   "Complete genome sequence of Weeksella virosa type strain (9751T).";
RL   Stand. Genomic Sci. 4:81-90(2011).
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; CP002455; ADX67861.1; -; Genomic_DNA.
DR   RefSeq; WP_013598251.1; NC_015144.1.
DR   AlphaFoldDB; F0P2M2; -.
DR   STRING; 865938.Weevi_1152; -.
DR   KEGG; wvi:Weevi_1152; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_2_0_10; -.
DR   OrthoDB; 9803729at2; -.
DR   Proteomes; UP000008641; 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.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:ADX67861.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008641}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   383 AA;  41744 MW;  B8AF9EB4667C6312 CRC64;
     MKFNTKTIHG GQQHDPSTGA VNPPIYQTST FAQQSPGKHK GYEYARGENP TRTALENSLA
     SIESGVAGFA FGSGLAAIDG ILKLFSPGDE IIAMDDLYGG SYRLFTRVYS NYGLKFHFVD
     MTNVDAIVDL MNDNTKMIWI ETPTNPLMKV VDIEAVSKAT KAKNANVLVA VDNTFASPYL
     QRPIELGADI VMHSATKYLG GHSDLVAGAV IVNSKELAEK VHFNLFATGG ILGPQDSYLV
     LRGIKTLAVR MDRHCENGMK IAEFLVQHPK VDKVYYPGLS NHPQHEIAKK QMKAFGGMVT
     FTLKSGKQED AFKLLENLKV FTLAESLGGV ESLANHPATM THASIPAEKR AEIGITDDLI
     RLSVGIEDID DLIEDLTNVF ALI
//
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