ID A0A160JFG1_9PROT Unreviewed; 392 AA.
AC A0A160JFG1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:ANC91625.1};
GN Name=metC {ECO:0000313|EMBL:ANC91625.1};
GN ORFNames=A6A40_06755 {ECO:0000313|EMBL:ANC91625.1};
OS Azospirillum humicireducens.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=1226968 {ECO:0000313|EMBL:ANC91625.1, ECO:0000313|Proteomes:UP000077405};
RN [1] {ECO:0000313|EMBL:ANC91625.1, ECO:0000313|Proteomes:UP000077405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SgZ-5 {ECO:0000313|EMBL:ANC91625.1,
RC ECO:0000313|Proteomes:UP000077405};
RX PubMed=23264502; DOI=10.1099/ijs.0.046813-0;
RA Zhou S., Han L., Wang Y., Yang G., Zhuang L., Hu P.;
RT "Azospirillum humicireducens sp. nov., a nitrogen-fixing bacterium isolated
RT from a microbial fuel cell.";
RL Int. J. Syst. Evol. Microbiol. 63:2618-2624(2013).
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}.
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DR EMBL; CP015285; ANC91625.1; -; Genomic_DNA.
DR RefSeq; WP_063634720.1; NZ_CP015285.1.
DR AlphaFoldDB; A0A160JFG1; -.
DR STRING; 1226968.A6A40_06755; -.
DR KEGG; ahu:A6A40_06755; -.
DR OrthoDB; 9790858at2; -.
DR Proteomes; UP000077405; Chromosome.
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 NCBIfam; TIGR01324; cysta_beta_ly_B; 1.
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 Lyase {ECO:0000313|EMBL:ANC91625.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 207
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 392 AA; 42195 MW; E66E7E15155E9870 CRC64;
MKDVTQDTIL VHAGRDPRNN HGIVNPPVYH CSTVLFPTLD ALEESDRNTL EGVHYGRMGT
PTTFAFEEAA AALEGGFKTV NTGSGLAAIA VALSAFTKAG DHVLITDSAY GPTRRFAKET
LAPYGVEVEF YDPCIGAGID ALLRSNTSVV FLESPGSLTF EVQDVPAIAA AAKKAGATVM
IDNTWATPLF FRPFDHGVDV SIHAATKYMV GHADAMLGVV TCRDEATWVA VKKAATRFGI
CGGPDDLYLG LRGLRTLSVR MRQHQESALA LADWLAARPE VTRVLHPARP DFPGHALWKR
DFTGSSGLFS IVINQVPRKA LAAMLDGMEL FGMGYSWGGF ESLILPTRPA AVRSATRWTD
PGQVLRLHAG LESADDLIRD LDAGFRRMAA AL
//
