ID F2IAK9_FLUTR Unreviewed; 762 AA. AC F2IAK9; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 71. 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=Fluta_1149 {ECO:0000313|EMBL:AEA43145.1}; OS Fluviicola taffensis (strain DSM 16823 / NCIMB 13979 / RW262). OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Crocinitomicaceae; Fluviicola. OX NCBI_TaxID=755732 {ECO:0000313|EMBL:AEA43145.1, ECO:0000313|Proteomes:UP000007463}; RN [1] {ECO:0000313|EMBL:AEA43145.1, ECO:0000313|Proteomes:UP000007463} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16823 / RW262 / RW262 {ECO:0000313|Proteomes:UP000007463}; RX PubMed=22180807; DOI=10.4056/sigs.2124912; RA Woyke T., Chertkov O., Lapidus A., Nolan M., Lucas S., Del Rio T.G., RA Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K., RA Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M., RA Mwirichia R., Sikorski J., Tindall B.J., Goker M., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of the gliding freshwater bacterium Fluviicola RT taffensis type strain (RW262)."; RL Stand. Genomic Sci. 5:21-29(2011). RN [2] {ECO:0000313|Proteomes:UP000007463} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16823 / RW262 / RW262 {ECO:0000313|Proteomes:UP000007463}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I., RA Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Fluviicola taffensis DSM 16823."; 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; CP002542; AEA43145.1; -; Genomic_DNA. DR RefSeq; WP_013685917.1; NC_015321.1. DR AlphaFoldDB; F2IAK9; -. DR STRING; 755732.Fluta_1149; -. DR KEGG; fte:Fluta_1149; -. DR eggNOG; COG0770; Bacteria. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_372082_0_0_10; -. DR OrthoDB; 9801978at2; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000007463; Chromosome. DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro. 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:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. 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; IPR004101; Mur_ligase_C. DR InterPro; IPR036615; Mur_ligase_C_dom_sf. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR035911; MurE/MurF_N. 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 Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 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 Cell cycle {ECO:0000256|ARBA:ARBA00023306}; KW Cell division {ECO:0000256|ARBA:ARBA00022618}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201}; KW Ligase {ECO:0000313|EMBL:AEA43145.1}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP- KW Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000007463}. FT DOMAIN 636..760 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT ACT_SITE 429 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT ACT_SITE 657 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT BINDING 529 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 706 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT MOD_RES 429 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-50" SQ SEQUENCE 762 AA; 85904 MW; 9293665D36C4ED50 CRC64; MRLNYSIEAC ASIFEATIIG SSSESITHIY FDSRKIQQAN GALFFALSGH SRSGNEFIEN AYQQGIRFFV IAKNASSKFH PDALYFQVEE PLTALQQLAT HHRKQYTYPV VAITGSVGKT TFKEWIFHCI SDKFKVVRSP KSFNSQIGVA LSLLEMHENA SIAFIEAGIS KPGEMKILRD MIQPDFGIFT AFGKAHRENF ADNEEHLLEK WTLFRECKLA FIPHTFADLE NRLPGNFQVC ESYENHHFPI GYSGMLGVLK TFLAYLQFES HQILERINSL PTLALRMEVF EGVNGNTIIN DTYNLDFDAL SEALIYQRQL APTKKRIVVI GLSEKHAHER LEIEKLITSF NPDEFHFIPE GKSIPWENFH NAVVLVKAHR DRAFEHEVAR GKALKHRTIV EINLSAIKHN VSFYQSRIPK EVKILAMVKA SSYGSGADKV APFLQQSGIR NFGVAFADEG VELRKAGIGI SSSIVVMNPD PEHSDLIIEY RLEPAIYSFE QLDEFITALI HKQISAYPIH LKFDTGMHRL GFAPSDKERI LAIINSQPEV KIQGIYSHLA DADNPIHSEF TQKQLTSFES IVSYFRTNSS DSFLAHILNS EGSLRYPESC YDMIRLGISM YGYTENNQLK ASLQGSVSWY SSISQIKAVP KGDFIGYGIS YQAIEDMTIA IIPVGYADGF RRSLSNGKGS VFIHGIKCPV VGRVCMDMIM VDISSVDAKI NDSVEIIGQN QPMEVFAKSM ETIPYEVMTG LSKRMHRVYV EE //