ID I2HSZ4_9BACI Unreviewed; 393 AA.
AC I2HSZ4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN ORFNames=MY7_2185 {ECO:0000313|EMBL:EIF13853.1};
OS Bacillus sp. 5B6.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1127743 {ECO:0000313|EMBL:EIF13853.1, ECO:0000313|Proteomes:UP000005799};
RN [1] {ECO:0000313|EMBL:EIF13853.1, ECO:0000313|Proteomes:UP000005799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5B6 {ECO:0000313|EMBL:EIF13853.1,
RC ECO:0000313|Proteomes:UP000005799};
RX PubMed=22740678; DOI=10.1128/JB.00682-12;
RA Kim B.K., Chung J.H., Kim S.Y., Jeong H., Kang S.G., Kwon S.K., Lee C.H.,
RA Song J.Y., Yu D.S., Ryu C.M., Kim J.F.;
RT "Genome Sequence of the Leaf-Colonizing Bacterium Bacillus sp. Strain 5B6,
RT Isolated from a Cherry Tree.";
RL J. Bacteriol. 194:3758-3759(2012).
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}.
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:EIF13853.1}.
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DR EMBL; AJST01000001; EIF13853.1; -; Genomic_DNA.
DR RefSeq; WP_007612500.1; NZ_AJST01000001.1.
DR AlphaFoldDB; I2HSZ4; -.
DR PATRIC; fig|1127743.3.peg.2142; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000005799; 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; 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}.
FT DOMAIN 250..378
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 39
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 272
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 39
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 393 AA; 43238 MW; 9CEC5DC268D6F4B9 CRC64;
MKKLCREVWI EVDLDAIKKN VRAIRRHIPN TSKIMAVVKA NAYGHGSVEV ARQALESGAS
ELAVASVEEG IVLRRAGITA PILVLGFTAL SCVKKSAVWN ITLSAFQVSW IKKANRILEK
EAESKRLSIH INVDTGMGRL GVRTEEDLLA VVKALKSSTY LSWDGIFTHF STADEPDTEL
TMLQHEKFIS FLSFLKNQDI TLPTVHMCNT AAAIAFPEFS ADMIRLGIGL YGLYPSASIK
ELNLVDLTPA LSLKARIAYV KAMVTDPRTV SYGATYIAEP GEIIATIPIG YADGYSRALS
NRGFILHRGR RVPVAGRVTM DMIMVSLGEN EGKQGEEVVI YGKQQGAEIS VDEIAEMLGT
ISYEVLSVLS RRVPRFYFRD GKIIKISAPV LYV
//
