ID A0A399G4Q2_9ACTN Unreviewed; 406 AA.
AC A0A399G4Q2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme {ECO:0000313|EMBL:UOE19712.1};
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:RII02570.1};
GN ORFNames=NI17_000095 {ECO:0000313|EMBL:UOE19712.1}, NI17_11205
GN {ECO:0000313|EMBL:RII02570.1};
OS Thermobifida halotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=483545 {ECO:0000313|EMBL:RII02570.1};
RN [1] {ECO:0000313|EMBL:RII02570.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44931 {ECO:0000313|EMBL:RII02570.1};
RA Toth A., Tancsics T.A., Farkas T., Papp P., Olasz F., Balint B.,
RA Herczeg R., Nagy I., Baka E., Kukolya J.;
RT "De novo genome project of the cellulose decomposer Thermobifida
RT halotolerans type strain.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:UOE19712.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44931 {ECO:0000313|EMBL:UOE19712.1};
RA Nagy I., Horvath B., Kukolya J., Nagy I., Orsini M.;
RT "De novo genome project of the cellulose decomposer Thermobifida
RT halotolerans type strain.";
RL Submitted (OCT-2020) 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; JRUV01000229; RII02570.1; -; Genomic_DNA.
DR EMBL; CP063196; UOE19712.1; -; Genomic_DNA.
DR RefSeq; WP_068687635.1; NZ_LIZN01000001.1.
DR AlphaFoldDB; A0A399G4Q2; -.
DR STRING; 483545.GCA_001660385_00316; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000265719; Chromosome.
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 Aminotransferase {ECO:0000313|EMBL:UOE19712.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000265719};
KW Transferase {ECO:0000313|EMBL:UOE19712.1}.
FT MOD_RES 212
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 406 AA; 42438 MW; 511D7C7A95E70E41 CRC64;
MAQQYGEHTR AVRTSTVAPE AGAPVRVPVY RTTTYAFETS QDYADALDRG DGYSYARIDA
PNSEAFASAV AELEGARLDH EVRGQAFASG MAAISTALLA LTRAGAHVVA SRAIYGNTHS
LLDGLLRRFG VETDFVDITD VDAVRAAVRP DTALVFTETL SNPGMLVSDL PALAAAAHEA
DALLVVDSTF ASPAVCRPLE HGADVVLHSA TKYLGGHSDA TGGVVVARPD LADRIRSARI
DLGPCLAADE AFLLHRGLET LPLRMARQCA TAAEFAAAVL RHPAVARVDH PSLPDHQGHE
LARKLFDTGP EGTRCGAVVT VTPRGGREAG TAFADGLRLA TIAASLGGTH TLVGHVASTS
HRQLSDEALR AAGIAPGAVR FSIGLEDPAD LIADALRALD ESPVKE
//
