ID A0A0F3IM65_9GAMM Unreviewed; 362 AA.
AC A0A0F3IM65;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Alanine racemase {ECO:0000256|ARBA:ARBA00013089, ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|ARBA:ARBA00013089, ECO:0000256|HAMAP-Rule:MF_01201};
GN Name=alr {ECO:0000313|EMBL:KJV07767.1};
GN ORFNames=VZ94_02590 {ECO:0000313|EMBL:KJV07767.1};
OS Methylocucumis oryzae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylocucumis.
OX NCBI_TaxID=1632867 {ECO:0000313|EMBL:KJV07767.1, ECO:0000313|Proteomes:UP000033684};
RN [1] {ECO:0000313|Proteomes:UP000033684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sn10-6 {ECO:0000313|Proteomes:UP000033684};
RA Pandit P.S., Pore S.D., Arora P., Kapse N.G., Dhakephalkar P.K.,
RA Rahalkar M.C.;
RT "Draft genome sequence of a novel methanotroph (Sn10-6) isolated from
RT flooded ricefield rhizosphere in India.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KJV07767.1, ECO:0000313|Proteomes:UP000033684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sn10-6 {ECO:0000313|EMBL:KJV07767.1,
RC ECO:0000313|Proteomes:UP000033684};
RX PubMed=26547566; DOI=10.1007/s00248-015-0699-z;
RA Rahalkar M.C., Pandit P.S., Dhakephalkar P.K., Pore S., Arora P., Kapse N.;
RT "Genome Characteristics of a Novel Type I Methanotroph (Sn10-6) Isolated
RT from a Flooded Indian Rice Field.";
RL Microb. Ecol. 71:519-523(2016).
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|ARBA:ARBA00037912,
CC ECO:0000256|HAMAP-Rule:MF_01201}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC Rule:MF_01201}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJV07767.1}.
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DR EMBL; LAJX01000018; KJV07767.1; -; Genomic_DNA.
DR RefSeq; WP_045778039.1; NZ_LAJX01000018.1.
DR AlphaFoldDB; A0A0F3IM65; -.
DR PATRIC; fig|1632867.3.peg.1910; -.
DR OrthoDB; 9813814at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000033684; Unassembled WGS sequence.
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; cd06827; PLPDE_III_AR_proteobact; 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:SF4; ALANINE RACEMASE, BIOSYNTHETIC; 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:UP000033684}.
FT DOMAIN 234..358
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 35
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 255
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 35
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 362 AA; 39669 MW; 29E32EDD566FFF9F CRC64;
MNPAAFAVLN LDALQHNLTI VRQQAPNAKI MAVIKGNGYG HGLLRVAEAL TNVDAFAVAR
VDEGMRLRKA GINNKIVVLE GFTSEQELNA LLAYRLDVLI HSFAQLDILS KRHERKQMGA
WLKIDTGMNR LGFKPIDFPS VYQQLKHSTI IKKPIRFMTH LANADDLNDV MTIKQIALFK
ETLANIPGER SIANSAGILG WPDALTDWVR PGVMLYGISP FPGRTGAEHG LKPIMEFHSR
LIAVKSVNSG ETVGYAGSWR CQQATTLGVV AVGYGDGYPR HATIGTPVLV NGQRVPLIGR
VSMDMITVDL AEQPNAKPGD PVTLWGKNLP VEEIAEHCNT IPYTLVCGIT QRVKQIDSAW
LV
//
