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Database: UniProt
Entry: A0A075K892_9FIRM
LinkDB: A0A075K892_9FIRM
Original site: A0A075K892_9FIRM 
ID   A0A075K892_9FIRM        Unreviewed;       374 AA.
AC   A0A075K892;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Cys/Met metabolism pyridoxal-phosphate-dependent protein {ECO:0000313|EMBL:AIF50471.1};
GN   ORFNames=UFO1_0916 {ECO:0000313|EMBL:AIF50471.1};
OS   Pelosinus sp. UFO1.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Pelosinus.
OX   NCBI_TaxID=484770 {ECO:0000313|EMBL:AIF50471.1, ECO:0000313|Proteomes:UP000027983};
RN   [1] {ECO:0000313|EMBL:AIF50471.1, ECO:0000313|Proteomes:UP000027983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UFO1 {ECO:0000313|EMBL:AIF50471.1};
RX   PubMed=25189589;
RA   Brown S.D., Utturkar S.M., Magnuson T.S., Ray A.E., Poole F.L.,
RA   Lancaster W.A., Thorgersen M.P., Adams M.W., Elias D.A.;
RT   "Complete Genome Sequence of Pelosinus sp. Strain UFO1 Assembled Using
RT   Single-Molecule Real-Time DNA Sequencing Technology.";
RL   Genome Announc. 2:e00881-14(2014).
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|RuleBase:RU362118}.
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DR   EMBL; CP008852; AIF50471.1; -; Genomic_DNA.
DR   RefSeq; WP_038668437.1; NZ_CP008852.1.
DR   AlphaFoldDB; A0A075K892; -.
DR   STRING; 484770.UFO1_0916; -.
DR   KEGG; puf:UFO1_0916; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_2_0_9; -.
DR   OrthoDB; 9803887at2; -.
DR   Proteomes; UP000027983; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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:SF93; CYSTATHIONINE GAMMA-LYASE-RELATED; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027983}.
FT   MOD_RES         196
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   374 AA;  40792 MW;  455E06A087CB2EF4 CRC64;
     MKIETKAIHL GHDVDPVTGA IAAPLHLSTT FEREADGSYP RGHIYTRLSN PNRDALEKCL
     AGLEGGEGAV AFASGLAAIM NVFQALSPKD HVIASQDLYH GTTHILQDIL EPWGLQVSFV
     DVTDLAQLEG AIQENTKIIY FETPSNPLLK ITDISRVAAI AHRIGALCVC DNTWPTPILQ
     RPLELGADIV VHSTTKYFGG HSDVLGGAVI SKVKDAFFDR IRMLQQIGGA VPAPFDCWLV
     LRGIQTLCCR MKNHSESAFA IADFLNKHPN VEKVYYPGLA DHPGHDIVLK QMSQFGGMLS
     FQIKGDKEEA LAFTGRLKII RRATSLGGVE SLIEHRASIE GPQSKTPDNL LRFSVGLENV
     DDLLTDLDDA LTKK
//
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