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Database: UniProt
Entry: H3SH32_9BACL
LinkDB: H3SH32_9BACL
Original site: H3SH32_9BACL 
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
//
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