ID A0A077M135_9MICO Unreviewed; 387 AA.
AC A0A077M135;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Cystathionine gamma-lyase and homocysteine gamma-lyase for reverse transsulfuration pathway {ECO:0000313|EMBL:CCH77920.1};
DE EC=4.4.1.- {ECO:0000313|EMBL:CCH77920.1};
DE EC=4.4.1.1 {ECO:0000313|EMBL:CCH77920.1};
GN Name=mccB {ECO:0000313|EMBL:CCH77920.1};
GN ORFNames=BN12_2380013 {ECO:0000313|EMBL:CCH77920.1};
OS Tetrasphaera japonica T1-X7.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1194083 {ECO:0000313|EMBL:CCH77920.1, ECO:0000313|Proteomes:UP000035721};
RN [1] {ECO:0000313|EMBL:CCH77920.1, ECO:0000313|Proteomes:UP000035721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T1-X7 {ECO:0000313|EMBL:CCH77920.1,
RC ECO:0000313|Proteomes:UP000035721};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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:CCH77920.1}.
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DR EMBL; CAJB01000155; CCH77920.1; -; Genomic_DNA.
DR RefSeq; WP_048554870.1; NZ_HF570958.1.
DR AlphaFoldDB; A0A077M135; -.
DR STRING; 1194083.BN12_2380013; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000035721; Unassembled WGS sequence.
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:CCH77920.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000035721}.
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 203
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 387 AA; 41061 MW; D0BE99F0E22AE6D3 CRC64;
MSDAPLGFSS RALHVGQDPD PTTGSVVTPI YQTSTYKQDG IGNLRGGYEY SRSANPTRTA
LEVLIASLEG GIRGYAFASG LAGQDTLLRA AVAPGDHVVI PTDAYGGTFR LFDKVLQPWG
LEYDIAPIAD VDAVRAAVRP GRTKILWVET PTNPLLGIAD IEALAGVAHE AGAILVVDNT
FASPYLQQPL ALGADVVTHS ATKYAGGHSD IVGGLVVVRE DEALAERIGF HQYAVGAIAG
PFDSWLVQRG LKTLALRMER HSDNAERVVE FLTGHPGVSK VHYPGLPEHP GHDVAARQMR
RFGGMVSFQV RAGEDVAVKV CGETQLWTLG ESLGGVESLI EHPARMTHAS VAGTELEVPA
DLIRLSVGIE DAEDLVADLA QALDRLA
//
