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Database: UniProt
Entry: D0MD89_RHOM4
LinkDB: D0MD89_RHOM4
Original site: D0MD89_RHOM4 
ID   D0MD89_RHOM4            Unreviewed;       332 AA.
AC   D0MD89;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Pyridoxal-5'-phosphate-dependent protein beta subunit {ECO:0000313|EMBL:ACY49001.1};
GN   OrderedLocusNames=Rmar_2122 {ECO:0000313|EMBL:ACY49001.1};
OS   Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS   obamensis).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae;
OC   Rhodothermus.
OX   NCBI_TaxID=518766 {ECO:0000313|EMBL:ACY49001.1, ECO:0000313|Proteomes:UP000002221};
RN   [1] {ECO:0000313|EMBL:ACY49001.1, ECO:0000313|Proteomes:UP000002221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43812 / DSM 4252 / R-10
RC   {ECO:0000313|Proteomes:UP000002221};
RX   PubMed=21304669; DOI=10.4056/sigs.46736;
RA   Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA   Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Detter J.C.;
RT   "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL   Stand. Genomic Sci. 1:283-291(2009).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; CP001807; ACY49001.1; -; Genomic_DNA.
DR   RefSeq; WP_012844612.1; NC_013501.1.
DR   AlphaFoldDB; D0MD89; -.
DR   STRING; 518766.Rmar_2122; -.
DR   KEGG; rmr:Rmar_2122; -.
DR   eggNOG; COG1171; Bacteria.
DR   HOGENOM; CLU_021152_4_2_10; -.
DR   OrthoDB; 9811476at2; -.
DR   Proteomes; UP000002221; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   CDD; cd01562; Thr-dehyd; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   PANTHER; PTHR43050; SERINE / THREONINE RACEMASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR43050:SF1; SERINE RACEMASE; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002221}.
FT   DOMAIN          23..307
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   332 AA;  35903 MW;  1EB249E106A85889 CRC64;
     MITLLPTYAD VEAAARRLEG VAHRTPVVRS RTLDRLTGAT LFFKCEHFQR AGSFKFRGAY
     NALATLPEAE RRRGVLTYSS GNHAQALALA GRLLGVRVTV VMPQNAPEVK RAATAGYGAE
     IVLYDPEQIT REELGRRLAA ERGLTIIPPY DHPQIVAGQG TAARELLEEV KSLDVLLVPC
     GGGGLLSGSA LSARALAPRC RVIGVEPERA DDATRSFRTG RLHRVHNPDT IADGARTPSL
     GEVTFPLVRQ YVDDMVTVSE TAILQAMYVL WERLKLVVEP TGALPLAALL ENRVAVKGRQ
     VGLILSGGNV DLRRAATLFA ELNQPPELPP SV
//
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