ID A7HLU1_FERNB Unreviewed; 364 AA. AC A7HLU1; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAR-2024, entry version 104. 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=Fnod_1025 {ECO:0000313|EMBL:ABS60874.1}; OS Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae; OC Fervidobacterium. OX NCBI_TaxID=381764 {ECO:0000313|EMBL:ABS60874.1, ECO:0000313|Proteomes:UP000002415}; RN [1] {ECO:0000313|EMBL:ABS60874.1, ECO:0000313|Proteomes:UP000002415} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1 RC {ECO:0000313|Proteomes:UP000002415}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.; RT "Complete sequence of Fervidobacterium nodosum Rt17-B1."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABS60874.1, ECO:0000313|Proteomes:UP000002415} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1 RC {ECO:0000313|Proteomes:UP000002415}; RX PubMed=19307556; DOI=10.1073/pnas.0901260106; RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M., RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P., RA Noll K.M.; RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of RT the Thermotogales."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009). 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; CP000771; ABS60874.1; -; Genomic_DNA. DR RefSeq; WP_011994188.1; NC_009718.1. DR AlphaFoldDB; A7HLU1; -. DR STRING; 381764.Fnod_1025; -. DR KEGG; fno:Fnod_1025; -. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_028393_2_2_0; -. DR OrthoDB; 9813814at2; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000002415; 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:UP000002415}. FT DOMAIN 232..360 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 253 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT BINDING 130 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 301 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 364 AA; 41302 MW; A0A1F4014D6CC6C3 CRC64; MESRRTYAVI NVRNYLDNLR FFQTHCAPAK VMPVVKANAY GHGAVQLAKA AQKIGIDYFA VAFLEEAIEL RKHGISKDIL VFNYIEPDLL HIAMENNITI TLYSWEQLWK YTKYVWRPKA HIKIDTGMRR LGVYPEEAKD FIESARNVGF EVEGAYTHFA VADSLDDEDV KFTQQQVEKF ANLNLDVKIK HLCNSGASVS KIVNCFDYVR VGIASYGLQP SDSVYSEQLK PVLSWKTTVS HVKTIQPGDS VSYGRTFKAF TEMRIATIPV GYADGYWRHL SNKGYVLIHG EKCPIIGRVC MDQFMVDVTH LEDVKIGDEV ILIGKQGDNI ITAEEIAKLV GTINYEVTCR ISERVPRKYE GLEL //