ID   F0R194_PHOSB            Unreviewed;       823 AA.
AC   F0R194;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   OrderedLocusNames=Bacsa_1763 {ECO:0000313|EMBL:ADY36322.1};
OS   Phocaeicola salanitronis (strain DSM 18170 / JCM 13657 / BL78) (Bacteroides
OS   salanitronis).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Phocaeicola.
OX   NCBI_TaxID=667015 {ECO:0000313|EMBL:ADY36322.1, ECO:0000313|Proteomes:UP000007486};
RN   [1] {ECO:0000313|EMBL:ADY36322.1, ECO:0000313|Proteomes:UP000007486}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18170 / JCM 13567 / BL78
RC   {ECO:0000313|Proteomes:UP000007486};
RX   PubMed=21677856; DOI=10.4056/sigs.1704212;
RA   Gronow S., Held B., Lucas S., Lapidus A., Del Rio T.G., Nolan M., Tice H.,
RA   Deshpande S., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA   Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brambilla E.M., Rohde M., Goker M., Detter J.C., Woyke T., Bristow J.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Eisen J.A.;
RT   "Complete genome sequence of Bacteroides salanitronis type strain (BL78).";
RL   Stand. Genomic Sci. 4:191-199(2011).
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, ECO:0000256|HAMAP-
CC         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}.
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DR   EMBL; CP002530; ADY36322.1; -; Genomic_DNA.
DR   RefSeq; WP_013617753.1; NC_015164.1.
DR   AlphaFoldDB; F0R194; -.
DR   STRING; 667015.Bacsa_1763; -.
DR   KEGG; bsa:Bacsa_1763; -.
DR   eggNOG; COG0770; Bacteria.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_372082_0_0_10; -.
DR   OrthoDB; 9801978at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000007486; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
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   Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 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; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR035911; MurE/MurF_N.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR005863; UDP-N-AcMur_synth.
DR   NCBIfam; TIGR00492; alr; 1.
DR   NCBIfam; TIGR01143; murF; 1.
DR   PANTHER; PTHR43024; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR43024:SF1; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW   Ligase {ECO:0000313|EMBL:ADY36322.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01201}.
FT   DOMAIN          697..821
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        493
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        718
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         591
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         767
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         493
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   823 AA;  92254 MW;  C68A424FB9320380 CRC64;
     MSSSIEEIVS VVGATRIGER QASISWILTD SRSLCFPEET LFFALKAKRN DGHKYIPELY
     ARGVYNFVVA EVPEEMKNCT DVNFLVVGNV LKALQRLAGK HREQYQVPVI GITGSNGKTV
     VKEWLYQLLS PDKRIIRSPR SYNSQIGVPL SVWMMDEHTE LGIFEAGISE MGEMETLEPI
     IRPTIGVLTN IGGAHQENFS SLQDKCMEKL LLFKECDVIV YNGDNELIRD CVSKSLFTAR
     EIAWSMKDPE RPLFIEKIEK DAAGTTIKYR YLGFFKEFRI PYIDDASIEN SLHCLAVALY
     LMVPTEVIAE RMAHLEPVAM RLEVKEGKNG CVLINDSYNS DFASLDIALD FMARRSEDKA
     RRRTLILSDI LETGQPGKLL YRQVAELVHS RGVDRLIGVG EEISASSSRF DVKEKQFFLT
     TEELMASGVL ETLRNDIVLI KGARAFHFDA VSDFLELKVH ETILEINLNA LVDNLNYYRN
     KLKPETKLMC MVKASAYGAG PFEVAKTLEE HRVDYLAVAV ADEGADLRKA GITCPIVIMN
     PEATAFKTMF AYRLEPNIYG FPILEEMIKA AEREGVSNFP IHIKIDTGMH RLGFSPHQDM
     QRLVERLHRQ SAVIPRSVFS HLAGSDSERF DAFTRKQIET FEAAAAELQA GFGVKILRHV
     CNTAGIERYP GAQFDMVRLG IGLYGIDPFT NHILHNVSTL KTTILQIHDI PADETVGYSR
     KGVLYRDSRI ATIPIGYADG LNRHLGNGHA YCLVNGKKAP YVGNICMDVC MIDVTDIDCK
     EGDKAIIFGD DLPVTVLAEA LGTIPYEILT SVSNRVKRVY FQG
//