ASRAC_PYRHO
ID ASRAC_PYRHO Reviewed; 474 AA.
AC O58478;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Alanine/serine racemase {ECO:0000303|PubMed:30038603};
DE Short=ASR {ECO:0000303|PubMed:30038603};
DE Short=Ala/Ser racemase {ECO:0000303|PubMed:30038603};
DE EC=5.1.1.- {ECO:0000269|PubMed:30038603};
DE EC=5.1.1.1 {ECO:0000269|PubMed:30038603};
GN OrderedLocusNames=PH0782 {ECO:0000312|EMBL:BAA29874.1};
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, COFACTOR, SUBUNIT, AND MUTAGENESIS OF ASP-251 AND LYS-308.
RX PubMed=30038603; DOI=10.3389/fmicb.2018.01481;
RA Kawakami R., Ohshida T., Sakuraba H., Ohshima T.;
RT "A novel PLP-dependent alanine/serine racemase from the hyperthermophilic
RT archaeon Pyrococcus horikoshii OT-3.";
RL Front. Microbiol. 9:1481-1481(2018).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine, and
CC L-serine and D-serine. Has weak activity with valine and threonine.
CC {ECO:0000269|PubMed:30038603}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC Evidence={ECO:0000269|PubMed:30038603};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = D-serine; Xref=Rhea:RHEA:10980, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:35247; Evidence={ECO:0000269|PubMed:30038603};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:30038603};
CC -!- ACTIVITY REGULATION: Completely inhibited by hydroxylamine
CC hydrochloride. {ECO:0000269|PubMed:30038603}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.3 mM for L-alanine {ECO:0000269|PubMed:30038603};
CC KM=4.5 mM for L-serine {ECO:0000269|PubMed:30038603};
CC KM=5.5 mM for D-alanine {ECO:0000269|PubMed:30038603};
CC KM=5.9 mM for D-serine {ECO:0000269|PubMed:30038603};
CC Vmax=28.2 umol/min/mg enzyme with L-alanine as substrate
CC {ECO:0000269|PubMed:30038603};
CC Vmax=31.4 umol/min/mg enzyme with L-serine as substrate
CC {ECO:0000269|PubMed:30038603};
CC Vmax=49.5 umol/min/mg enzyme with D-alanine as substrate
CC {ECO:0000269|PubMed:30038603};
CC Vmax=41.2 umol/min/mg enzyme with D-serine as substrate
CC {ECO:0000269|PubMed:30038603};
CC pH dependence:
CC Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:30038603};
CC Temperature dependence:
CC Highly stable at high temperatures. {ECO:0000269|PubMed:30038603};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:30038603}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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; BA000001; BAA29874.1; -; Genomic_DNA.
DR PIR; H71126; H71126.
DR AlphaFoldDB; O58478; -.
DR SMR; O58478; -.
DR STRING; 70601.3257191; -.
DR EnsemblBacteria; BAA29874; BAA29874; BAA29874.
DR KEGG; pho:PH0782; -.
DR eggNOG; arCOG00915; Archaea.
DR OMA; PLVPYNA; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0030378; F:serine racemase activity; IEA:RHEA.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Isomerase; Pyridoxal phosphate.
FT CHAIN 1..474
FT /note="Alanine/serine racemase"
FT /id="PRO_0000448757"
FT BINDING 139..140
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P22256"
FT BINDING 282
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P22256"
FT BINDING 336
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P22256"
FT MOD_RES 308
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P22256"
FT MUTAGEN 251
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:30038603"
FT MUTAGEN 308
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:30038603"
SQ SEQUENCE 474 AA; 52570 MW; AA381FFCBAF93BBB CRC64;
MPFLPFSYYP FSLEVILMEY PKIVVKPPGP RAKELIEREK KVLSTGIGVK LFPLVPKRGF
GPFIEDVDGN VFIDFLAGAA AASTGYAHPK LVKAVKEQVE LIQHSMIGYT HSERAIRVAE
KLVEISPIEN SKVIFGLSGS DAVDMAIKVS KFSTRRPWIL AFIGAYHGQT LGATSVASFQ
VSQKRGYSPL MPNVFWIPYP NPFRNIWGIN GYEEPDELIN RVLDYLEYYV FSHVVPPDEV
AALFAEPIQG DAGIVVPPEN FFKELKKLLE EYGILLVMDE VQTGIGRTGK WFASEWFNVK
PDMIIFGKGV ASGMGLSGVI GRKEIMDITS GSALLTPAAN PVISAAAEAT LEIIEEENLL
KNALEVGEFI MGRLKEIKER FEIIGDVRGK GLMIGVEIVK ENGRPDPEMT GKICWRAFEL
GLILPSYGMF GNVIRITPPL VLTKEVAEKA LEIIERAIKD TLTGKVERKV VTWH
