ID F0SXB6_SYNGF Unreviewed; 376 AA. AC F0SXB6; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 74. 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=Sgly_2703 {ECO:0000313|EMBL:ADY56976.1}; OS Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae; OC Syntrophobotulus. OX NCBI_TaxID=645991 {ECO:0000313|EMBL:ADY56976.1, ECO:0000313|Proteomes:UP000007488}; RN [1] {ECO:0000313|EMBL:ADY56976.1, ECO:0000313|Proteomes:UP000007488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488}; RX PubMed=21886864; RA Han C., Mwirichia R., Chertkov O., Held B., Lapidus A., Nolan M., Lucas S., RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S., RA Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K., RA Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Brambilla E.M., Rohde M., Spring S., Sikorski J., Goker M., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P., Detter J.C.; RT "Complete genome sequence of Syntrophobotulus glycolicus type strain RT (FlGlyR)."; RL Stand. Genomic Sci. 4:371-380(2011). RN [2] {ECO:0000313|Proteomes:UP000007488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488}; RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., RA Chertkov O., Held B., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Syntrophobotulus glycolicus DSM 8271."; RL Submitted (FEB-2011) 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, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002547; ADY56976.1; -; Genomic_DNA. DR RefSeq; WP_013625796.1; NC_015172.1. DR AlphaFoldDB; F0SXB6; -. DR STRING; 645991.Sgly_2703; -. DR KEGG; sgy:Sgly_2703; -. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_028393_2_2_9; -. DR OrthoDB; 9813814at2; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000007488; Chromosome. 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}; Reference proteome {ECO:0000313|Proteomes:UP000007488}. FT DOMAIN 241..369 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT ACT_SITE 36 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT ACT_SITE 262 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT BINDING 134 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 310 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT MOD_RES 36 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-50" SQ SEQUENCE 376 AA; 41495 MW; 2EF60465963781AD CRC64; MHGMRPAWAC IDLGALRRNY RRICRQTNSE VMAIVKANAY GHGALEIVRT LKEEGVRRFG VAILEEALQI REKFPEVTVM LIGPTMPDQA ERIVAEGIIP EVFRLEQAEA FSLEAEKKGI PAILHIKVDT GMGRIGFQED ALENILKIAQ LPGIEIEGIY THLATADEID LGFAFTQLKR FDGLYESLKT AGLNIPMRHV ANSAAILQLR DQEYELCRPG LMLYGQLPMN HWEGENGFEP LMSLKARIVH LKKIAAGDSV SYGRTFIAQA PTLVATLPLG YADGLRRSLS NNWNVIVKGR YAPVIGRICM DQTMIDVTGI EGVEIGDEVT ILGSEGKSSL TAAQMAECAG TISYEILCGI SQRVPRVYID TSQIPK //