ALR_CORGL
ID ALR_CORGL Reviewed; 361 AA.
AC Q8RSU9;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN Name=alr; OrderedLocusNames=Cgl0588, cg0681;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12204559; DOI=10.1016/s0168-1656(02)00159-1;
RA Tauch A., Goetker S., Puehler A., Kalinowski J., Thierbach G.;
RT "The alanine racemase gene alr is an alternative to antibiotic resistance
RT genes in cloning systems for industrial Corynebacterium glutamicum
RT strains.";
RL J. Biotechnol. 99:79-91(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP COFACTOR, SUBUNIT, AND PYRIDOXAL PHOSPHATE AT LYS-34.
RA Miyaguchi I., Sasaki C., Kato R., Oikawa T., Sugio S.;
RT "Crystal structure of alanine racemase from Corynebacterium glutamicum at
RT 2.1 A resolution.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC also act on other amino acids. {ECO:0000255|HAMAP-Rule:MF_01201}.
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:0000255|HAMAP-Rule:MF_01201};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01201, ECO:0000269|Ref.4};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01201}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.4}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP-
CC Rule:MF_01201}.
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DR EMBL; AY077456; AAL77207.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB97981.1; -; Genomic_DNA.
DR EMBL; BX927149; CAF19293.1; -; Genomic_DNA.
DR RefSeq; NP_599824.1; NC_003450.3.
DR RefSeq; WP_011013748.1; NC_006958.1.
DR PDB; 2DY3; X-ray; 2.10 A; A/B/C/D=1-361.
DR PDBsum; 2DY3; -.
DR AlphaFoldDB; Q8RSU9; -.
DR SMR; Q8RSU9; -.
DR STRING; 196627.cg0681; -.
DR KEGG; cgb:cg0681; -.
DR KEGG; cgl:Cgl0588; -.
DR PATRIC; fig|196627.13.peg.579; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_0_0_11; -.
DR OMA; WEILCGF; -.
DR UniPathway; UPA00042; UER00497.
DR EvolutionaryTrace; Q8RSU9; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..361
FT /note="Alanine racemase"
FT /id="PRO_0000114512"
FT ACT_SITE 34
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 256
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 304
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT MOD_RES 34
FT /note="N6-(pyridoxal phosphate)lysine"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:2DY3"
FT HELIX 10..24
FT /evidence="ECO:0007829|PDB:2DY3"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:2DY3"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:2DY3"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:2DY3"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:2DY3"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:2DY3"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:2DY3"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:2DY3"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:2DY3"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:2DY3"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:2DY3"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:2DY3"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:2DY3"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:2DY3"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:2DY3"
FT HELIX 170..186
FT /evidence="ECO:0007829|PDB:2DY3"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:2DY3"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:2DY3"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:2DY3"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:2DY3"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:2DY3"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:2DY3"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:2DY3"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:2DY3"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:2DY3"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:2DY3"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:2DY3"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:2DY3"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:2DY3"
FT HELIX 334..340
FT /evidence="ECO:0007829|PDB:2DY3"
FT HELIX 345..350
FT /evidence="ECO:0007829|PDB:2DY3"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:2DY3"
SQ SEQUENCE 361 AA; 39174 MW; 6E95CAF6456B6037 CRC64;
MNLLTTKIDL DAIAHNTRVL KQMAGPAKLM AVVKANAYNH GVEKVAPVIA AHGADAFGVA
TLAEAMQLRD IGISQEVLCW IWTPEQDFRA AIDRNIDLAV ISPAHAKALI ETDAEHIRVS
IKIDSGLHRS GVDEQEWEGV FSALAAAPHI EVTGMFTHLA CADEPENPET DRQIIAFRRA
LALARKHGLE CPVNHVCNSP AFLTRSDLHM EMVRPGLAFY GLEPVAGLEH GLKPAMTWEA
KVSVVKQIEA GQGTSYGLTW RAEDRGFVAV VPAGYADGMP RHAQGKFSVT IDGLDYPQVG
RVCMDQFVIS LGDNPHGVEA GAKAVIFGEN GHDATDFAER LDTINYEVVC RPTGRTVRAY
V
