ID A5GVZ1_SYNR3 Unreviewed; 395 AA.
AC A5GVZ1;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN Name=alr {ECO:0000313|EMBL:CAK29050.1};
GN OrderedLocusNames=SynRCC307_2147 {ECO:0000313|EMBL:CAK29050.1};
OS Synechococcus sp. (strain RCC307).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK29050.1, ECO:0000313|Proteomes:UP000001115};
RN [1] {ECO:0000313|EMBL:CAK29050.1, ECO:0000313|Proteomes:UP000001115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG Genoscope;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC also act on other amino acids. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01201};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC Rule:MF_01201}.
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DR EMBL; CT978603; CAK29050.1; -; Genomic_DNA.
DR AlphaFoldDB; A5GVZ1; -.
DR STRING; 316278.SynRCC307_2147; -.
DR KEGG; syr:SynRCC307_2147; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_2_2_3; -.
DR OrthoDB; 9813814at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000001115; 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 CDD; cd00430; PLPDE_III_AR; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 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 NCBIfam; TIGR00492; alr; 1.
DR PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
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; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000001115}.
FT DOMAIN 260..388
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 54
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 281
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 54
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 395 AA; 42591 MW; 33EBBF5EA72C6D82 CRC64;
MQHESLPGLT REMIPSVQPQ QRAWLEIDRD AIRYNTAQLK GSLSPGCALM AVVKADGYGH
GAVTVAEAAL DGGASSFGVA TLAEGIELRQ AGIEAPILVL GNLQQPEEFR CCLHWQLSPT
ISSLRQGLIG SNVGVAGGKP LLAHLKLDTG MARLGIDWQQ GPKLLEELQQ LDGLSIAGVY
SHLADADNPD GLLNATQQER FEAVLRRFHE LELKPGLRHL ANSAGTLSSP ELHYDMVRVG
LSLYGHSPAA HLKQLPLRPA MSVHAKVTLL RDVPAGAGVS YGHQFHTTRP SRLAVLGIGY
ADGVSRRLSG QMEVLAEGRR LPQVGAITMD QIVIDATDLP ELDIGDSVTL LGSSGSETIG
PQAWSDVCQS IPWEVLCSFK HRLPRLPRLP RRPEH
//
