ID D2BBB7_STRRD Unreviewed; 371 AA.
AC D2BBB7;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 88.
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=Sros_1141 {ECO:0000313|EMBL:ACZ84140.1};
OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS 9100).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Streptosporangium.
OX NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ84140.1, ECO:0000313|Proteomes:UP000002029};
RN [1] {ECO:0000313|EMBL:ACZ84140.1, ECO:0000313|Proteomes:UP000002029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC {ECO:0000313|Proteomes:UP000002029};
RX PubMed=21304675; DOI=10.4056/sigs.631049;
RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Streptosporangium roseum type strain (NI
RT 9100).";
RL Stand. Genomic Sci. 2:29-37(2010).
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 alanine racemase family. {ECO:0000256|HAMAP-
CC Rule:MF_01201}.
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DR EMBL; CP001814; ACZ84140.1; -; Genomic_DNA.
DR AlphaFoldDB; D2BBB7; -.
DR STRING; 479432.Sros_1141; -.
DR KEGG; sro:Sros_1141; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_0_0_11; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000002029; 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:UP000002029}.
FT DOMAIN 244..371
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 34
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 265
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 34
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 371 AA; 38589 MW; 5B0E1CE580126ECF CRC64;
MTPAEARVDL SAIRDNVALL GEHAPGAEIM VVVKADGYGH GMAACGRAAL EGGATRLGTA
YIREALELRA AGVTAPILSW IIPPGEPLDE AVGQGVELSA GTPALVDEIA AAAGRTGVAA
RVHLKADTGL ARGGAAPADW PALVDRAMAR QFEGTIEVAG LWSHFACADI PGHPSVHAQL
TAFDDALAIA EKAGAGGSHV IRHIANSAAT MLLPQAHYDM VRPGLATYGL SPVPELGGFG
LRPAMTLVAR IALAKRVPVG SGVSYGHLYV TERETTLGLV PLGYADGILR HATNRAEVLA
GGRRRRIAGR VCMDQFVIDV GDDPLAEGDE VILFGDGSRG EPTAQEWADS LGTITHEIVT
RIGSRVPRVY R
//
