ID H3SH32_9BACL Unreviewed; 629 AA.
AC H3SH32;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
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=PDENDC454_14197 {ECO:0000313|EMBL:EHQ61650.1};
OS Paenibacillus dendritiformis C454.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ61650.1, ECO:0000313|Proteomes:UP000003900};
RN [1] {ECO:0000313|EMBL:EHQ61650.1, ECO:0000313|Proteomes:UP000003900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C454 {ECO:0000313|EMBL:EHQ61650.1,
RC ECO:0000313|Proteomes:UP000003900};
RX PubMed=22461558; DOI=10.1128/JB.00158-12;
RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA Gutnick D.L., Lancet D., Ben-Jacob E.;
RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT dendritiformis C454 Chiral Morphotype.";
RL J. Bacteriol. 194:2127-2128(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 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:EHQ61650.1}.
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DR EMBL; AHKH01000033; EHQ61650.1; -; Genomic_DNA.
DR RefSeq; WP_006677341.1; NZ_AHKH01000033.1.
DR AlphaFoldDB; H3SH32; -.
DR STRING; 1131935.PDENDC454_14197; -.
DR PATRIC; fig|1131935.3.peg.2942; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000003900; 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}; Reference proteome {ECO:0000313|Proteomes:UP000003900};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 38..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 500..629
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 294
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 521
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 570
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 294
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 629 AA; 69505 MW; 6FB2BECB32048263 CRC64;
MTANVHVGGL DRFKIVAALL VIAIHTGPLM SYSSYADFLL TGIAARVAVP LFFIASGFLF
FRKLTGEASR DRALLHRFMR RIGLLYAVSI VLYLPLNGYA GYFAGDFNLM SLLRDLVFNG
TFYHLWYLPA LFLGTYITYF LYRTLPLQGM LAAAGLLYIA GLLGDSYYGV TEQLPVLRAA
YARMFTWFDY TRNGLFFAPL YIALGAWTAA RSVRLRSAAA GAGLLLLRQT DGRGTALSVM
MSFGVIRFLG RFRRASPDLR RRAWAEIRLD DVTHNVRELR GLLPPDCELM AVVKADAYGH
GSIPVARHLS RIGVRQFAVA DVEEGVALRR EGIKGEILVL GYTSPERFDD LARYRLTQTV
INADYGKALD AFGKYVNVHI KIDTGMSRLG ERWSHTDEIC SMYRLRKVRV TGTFTHLSSC
DSPAEADIAF TNAQIKRFRE TIDQIKAAGL DPGTLHMQSS YGIVNYPELH CGMARPGIAL
FGLLGTERDQ AQAPIDLRPA LSWRARVTLV KQMQADEPVG YGRNYKTRTG SVIATVSIGY
ADGVPRVLAE KGGAVLIRGQ RAPIAGNICM DQFMVDVTHI GGVQEGDTVT LIGQDGEASI
TAGEMARRCG TITNEIVSRI GQRVDRIYL
//