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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//