ALR1_SCHPO
ID ALR1_SCHPO Reviewed; 375 AA.
AC O59828;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Alanine racemase, catabolic;
DE EC=5.1.1.1 {ECO:0000269|PubMed:11244061};
GN Name=alr1; ORFNames=SPCC965.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=SP1;
RX PubMed=11244061; DOI=10.1128/jb.183.7.2226-2233.2001;
RA Uo T., Yoshimura T., Tanaka N., Takegawa K., Esaki N.;
RT "Functional characterization of alanine racemase from Schizosaccharomyces
RT pombe: a eucaryotic counterpart to bacterial alanine racemase.";
RL J. Bacteriol. 183:2226-2233(2001).
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:11244061};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:11244061};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.0 mM for L-alanine {ECO:0000269|PubMed:11244061};
CC KM=2.4 mM for D-alanine {ECO:0000269|PubMed:11244061};
CC Vmax=679 umol/min/mg enzyme with L-alanine as substrate
CC {ECO:0000269|PubMed:11244061};
CC Vmax=350 umol/min/mg enzyme with D-alanine as substrate
CC {ECO:0000269|PubMed:11244061};
CC pH dependence:
CC Optimum pH is 9.0-9.5. {ECO:0000269|PubMed:11244061};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000305}.
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DR EMBL; CU329672; CAA19068.1; -; Genomic_DNA.
DR PIR; T41661; T41661.
DR RefSeq; NP_588518.1; NM_001023507.2.
DR AlphaFoldDB; O59828; -.
DR SMR; O59828; -.
DR BioGRID; 275325; 1.
DR STRING; 4896.SPCC965.08c.1; -.
DR PaxDb; O59828; -.
DR PRIDE; O59828; -.
DR EnsemblFungi; SPCC965.08c.1; SPCC965.08c.1:pep; SPCC965.08c.
DR GeneID; 2538742; -.
DR KEGG; spo:SPCC965.08c; -.
DR PomBase; SPCC965.08c; alr1.
DR VEuPathDB; FungiDB:SPCC965.08c; -.
DR eggNOG; ENOG502S6C6; Eukaryota.
DR HOGENOM; CLU_028393_1_0_1; -.
DR InParanoid; O59828; -.
DR PhylomeDB; O59828; -.
DR BRENDA; 5.1.1.1; 5613.
DR UniPathway; UPA00042; UER00497.
DR PRO; PR:O59828; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008784; F:alanine racemase activity; IDA:PomBase.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0030378; F:serine racemase activity; IDA:PomBase.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0055130; P:D-alanine catabolic process; IDA:PomBase.
DR GO; GO:0036088; P:D-serine catabolic process; IDA:PomBase.
DR Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 1.
DR HAMAP; MF_01201; Ala_racemase; 1.
DR InterPro; IPR000821; Ala_racemase.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR011079; Ala_racemase_C.
DR InterPro; IPR001608; Ala_racemase_N.
DR InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR InterPro; IPR029066; PLP-binding_barrel.
DR Pfam; PF00842; Ala_racemase_C; 1.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR PRINTS; PR00992; ALARACEMASE.
DR SMART; SM01005; Ala_racemase_C; 1.
DR SUPFAM; SSF50621; SSF50621; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
DR TIGRFAMs; TIGR00492; alr; 1.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 1: Evidence at protein level;
KW Isomerase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..375
FT /note="Alanine racemase, catabolic"
FT /id="PRO_0000114604"
FT ACT_SITE 38
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000250"
FT ACT_SITE 269
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000250"
FT MOD_RES 38
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 375 AA; 41585 MW; 76CEBD17E159E13F CRC64;
MRGAKSVIDL HAIAHNYNVA KQMMLQKNPS GHVLAIVKAN AYGHGAVQVA RFLLKHCSSI
DGFGVSSIEE ALELRHGGIY NKIVLLEGFF TEEDELKLID DYNFSIIIHS EDQVNSFIKY
PFNRPVEIWL KLDSGMNRLG FTPSQFMKFY NLLSNNKNVS NIGKITHFAF ADMLENPEHT
LKQWDIFEKS VAHLPGPLSA GGSAIILGWL NTVCTDWLRA GIMLYGISPF LSKNKDSKTP
ESVNIKPAMK LVSTIISVKH VDKGQPIGYG GRYVATRDMK LGVVAMGYGD GFPRQVKDGC
PVLVNGVKAP IVGRVSMDML TVDLSDIPDV KPGDEVIFWG TPELTVADIA KYCSDTSPYE
LVTKLTRRVP LQYTY
