HYDRA_PAEAU
ID HYDRA_PAEAU Reviewed; 236 AA.
AC Q9F466;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Hydantoin racemase {ECO:0000303|PubMed:10949312};
DE EC=5.1.99.5 {ECO:0000269|PubMed:10949312};
GN Name=hyuA {ECO:0000303|PubMed:10949312};
OS Paenarthrobacter aurescens (Arthrobacter aurescens).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=43663;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MASS SPECTROMETRY,
RP SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=DSM 3747;
RX PubMed=10949312; DOI=10.1016/s0168-1656(00)00262-5;
RA Wiese A., Pietzsch M., Syldatk C., Mattes R., Altenbuchner J.;
RT "Hydantoin racemase from Arthrobacter aurescens DSM 3747: heterologous
RT expression, purification and characterization.";
RL J. Biotechnol. 80:217-230(2000).
CC -!- FUNCTION: Involved in the asymmetric conversion of racemic 5-
CC substituted hydantoins to the corresponding L-amino acids. Catalyzes
CC the racemization via enolization of D- and L-5-monosubstituted
CC hydantoins. It shows preference for hydantoins with arylalkyl side
CC chains such as 5-benzyl-hydantoin (BH) and 5-(3-indolymethylene)-
CC hydantoin (IMH). {ECO:0000269|PubMed:10949312}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-5-monosubstituted hydantoin = a L-5-monosubstituted
CC hydantoin; Xref=Rhea:RHEA:46624, ChEBI:CHEBI:86339,
CC ChEBI:CHEBI:86340; EC=5.1.99.5;
CC Evidence={ECO:0000269|PubMed:10949312};
CC -!- ACTIVITY REGULATION: Completely inhibited by HgCl(2) and iodoacetamide.
CC Stimulated by dithiothreitol. {ECO:0000269|PubMed:10949312}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:10949312};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:10949312};
CC -!- SUBUNIT: Homohexamer, homoheptamer or homooctamer.
CC {ECO:0000269|PubMed:10949312}.
CC -!- MASS SPECTROMETRY: Mass=25078; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10949312};
CC -!- SIMILARITY: Belongs to the HyuE racemase family. {ECO:0000305}.
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DR EMBL; AF146701; AAG02129.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9F466; -.
DR SMR; Q9F466; -.
DR BioCyc; MetaCyc:MON-13960; -.
DR GO; GO:0036348; F:hydantoin racemase activity; ISS:UniProtKB.
DR GO; GO:0036361; F:racemase activity, acting on amino acids and derivatives; IEA:InterPro.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR015942; Asp/Glu/hydantoin_racemase.
DR Pfam; PF01177; Asp_Glu_race; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Coiled coil; Isomerase.
FT CHAIN 1..236
FT /note="Hydantoin racemase"
FT /id="PRO_0000439847"
FT SITE 77
FT /note="Seems to be responsible for recognition and proton
FT retrieval of D-isomers"
FT /evidence="ECO:0000250|UniProtKB:Q6TMG4"
FT SITE 182
FT /note="Seems to be responsible for L-isomers recognition
FT and racemization"
FT /evidence="ECO:0000250|UniProtKB:Q6TMG4"
SQ SEQUENCE 236 AA; 25086 MW; 8265D3499B632B74 CRC64;
MRILVINPNS SSALTESVAD AAQQVVATGT IISAINPSRG PAVIEGSFDE ALATFHLIEE
VERAERENPP DAYVIACFGD PGLDAVKELT DRPVVGVAEA AIHMSSFVAA TFSIVSILPR
VRKHLHELVR QAGATNRLAS IKLPNLGVMA FHEDEHAALE TLKQAAKEAV QEDGAESIVL
GCAGMVGFAR QLSDELGVPV IDPVEAACRV AESLVALGYQ TSKANSYQKP TEKQYL
