ID W8YT07_9BACL Unreviewed; 713 AA.
AC W8YT07;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=vanTG {ECO:0000313|EMBL:CDN42715.1};
GN ORFNames=BN871_BV_00120 {ECO:0000313|EMBL:CDN42715.1};
OS Paenibacillus sp. P22.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=483908 {ECO:0000313|EMBL:CDN42715.1, ECO:0000313|Proteomes:UP000035761};
RN [1] {ECO:0000313|EMBL:CDN42715.1, ECO:0000313|Proteomes:UP000035761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P22 {ECO:0000313|EMBL:CDN42715.1,
RC ECO:0000313|Proteomes:UP000035761};
RA Rattei T.;
RL Submitted (MAR-2014) 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 acyltransferase 3 family.
CC {ECO:0000256|ARBA:ARBA00007400}.
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:CDN42715.1}.
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DR EMBL; CBRA020000048; CDN42715.1; -; Genomic_DNA.
DR RefSeq; WP_048745399.1; NZ_CBRA020000048.1.
DR AlphaFoldDB; W8YT07; -.
DR STRING; 483908.BN871_BV_00120; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000035761; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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; 3.20.20.10; Alanine racemase; 1.
DR HAMAP; MF_01201; Ala_racemase; 1.
DR InterPro; IPR002656; Acyl_transf_3_dom.
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; PF01757; Acyl_transf_3; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01201}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 583..712
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 377
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 604
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 471
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 653
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 377
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 713 AA; 76912 MW; CEFD9035462781D2 CRC64;
MAAEARFGSL DRFKLLAGLL VVANHTSPLT TYSPFADFLL SGLLSRVAVP FFFMASGFFF
FRSLPRKPSR WAALKQFMSR IGFLYAVGIL LYLPLNVYSG DFNSSRNFGS YVSGLFFNGT
FYHLWYLPAL MIGVGIVFGL KAALPGKAVI GIAAGLYAIG LLGDSYFGLT ASVSPALAAV
FNSSFHWSDY TRNGIWFAPL FIAMGAGAAQ RPLPPASAPK LAVAFLFFLA LTLIEGIWLK
QADFARLGAM YVFLVPAMYS LFHLLLRLGG KKSLLLRQLS TWIYVVHPWM IVAVRGTAKL
LGLQALLIGN SLIHFIAVAA TSAALSLGGV IMLTKLKSTT AARSRAWAEI DLANLDHNVK
ELQRILPSGT ALMAVVKANA YGHGAAPVAE RLYSAGISSF AVAEIDEGIA MRRQGIQGEI
LVLGYTPSDR LDELLHADLA QTVVSAEDAE RLQASGKRIN VHIKIDTGMN RLGEPFGHTE
KILSMYRHSH LHVIGTFSHL ACADSPDEED RAFTRLQYER LLEVAAKIRS AGHDPGRLHI
QNSSGILNGF GWSFDTARPG LALYGLNSAP EGRIPADIEL RPVLSLKASV TRVSRVECGE
AVGYNRGFTA SRATVLATLS IGYADGIPRR LAETGGSVLL HGKRAPIVGR ISMDQMTVDV
TEIEGVRQGD AATLIGRDGA EAIAAEEVAA SAGTIVNEVL SRLGPRLQRI YLS
//
