ID ACLR_ACHOB Reviewed; 436 AA. AC Q7M181; DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 72. DE RecName: Full=2-aminohexano-6-lactam racemase; DE EC=5.1.1.15; DE AltName: Full=2-amino-hexano-6-lactam racemase; DE AltName: Full=Alpha-amino-epsilon-caprolactam racemase; OS Achromobacter obae. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=37486; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Naoko N., Oshihara W., Yanai A.; RT "Alpha-amino-epsilon-caprolactam racemase for L-lysine production."; RL (In) Korpela T., Christen P. (eds.); RL Biochemistry of Vitamin B6, pp.449-452, Birkhauser Verlag, Basel (1987). RN [2] RP CATALYTIC ACTIVITY. RX PubMed=3955003; DOI=10.1021/bi00350a017; RA Ahmed S.A., Esaki N., Tanaka H., Soda K.; RT "Mechanism of alpha-amino-epsilon-caprolactam racemase reaction."; RL Biochemistry 25:385-388(1986). RN [3] RP IDENTIFICATION. RX PubMed=24826896; DOI=10.1371/journal.pone.0097250; RA Shearer A.G., Altman T., Rhee C.D.; RT "Finding sequences for over 270 orphan enzymes."; RL PLoS ONE 9:E97250-E97250(2014). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE RP AND EPSILON-CAPROLACTAM, PYRIDOXAL PHOSPHATE AT LYS-267, ACTIVE SITE, RP FUNCTION, AND SUBUNIT. RX PubMed=19146406; DOI=10.1021/bi801574p; RA Okazaki S., Suzuki A., Mizushima T., Kawano T., Komeda H., Asano Y., RA Yamane T.; RT "The novel structure of a pyridoxal 5'-phosphate-dependent fold-type I RT racemase, alpha-amino-epsilon-caprolactam racemase from Achromobacter RT obae."; RL Biochemistry 48:941-950(2009). CC -!- FUNCTION: catalyzes the interconversion of L-alpha-amino-epsilon- CC caprolactam and D-alpha-amino-epsilon-caprolactam. CC {ECO:0000269|PubMed:19146406}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-2-aminohexano-6-lactam = D-2-aminohexano-6-lactam; CC Xref=Rhea:RHEA:14813, ChEBI:CHEBI:58113, ChEBI:CHEBI:58609; CC EC=5.1.1.15; Evidence={ECO:0000269|PubMed:3955003}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000305}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19146406}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. 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 PIR; JC1497; JC1497. DR PDB; 2ZUK; X-ray; 2.41 A; A/B=1-436. DR PDB; 3DXV; X-ray; 2.21 A; A/B=1-436. DR PDB; 3DXW; X-ray; 2.41 A; A/B=1-436. DR PDBsum; 2ZUK; -. DR PDBsum; 3DXV; -. DR PDBsum; 3DXW; -. DR AlphaFoldDB; Q7M181; -. DR SMR; Q7M181; -. DR BRENDA; 5.1.1.10; 76. DR BRENDA; 5.1.1.15; 76. DR EvolutionaryTrace; Q7M181; -. DR GO; GO:0047463; F:2-aminohexano-6-lactam racemase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:InterPro. DR CDD; cd00610; OAT_like; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR049704; Aminotrans_3_PPA_site. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1. DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Isomerase; Pyridoxal phosphate. FT CHAIN 1..436 FT /note="2-aminohexano-6-lactam racemase" FT /id="PRO_0000430444" FT ACT_SITE 137 FT /evidence="ECO:0000305|PubMed:19146406" FT BINDING 110..111 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT BINDING 137 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000250" FT BINDING 238..241 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000250" FT BINDING 295 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000269|PubMed:19146406" FT MOD_RES 267 FT /note="N6-(pyridoxal phosphate)lysine" FT HELIX 5..12 FT /evidence="ECO:0007829|PDB:3DXV" FT HELIX 15..17 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 25..31 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 33..36 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 41..46 FT /evidence="ECO:0007829|PDB:3DXV" FT TURN 47..51 FT /evidence="ECO:0007829|PDB:3DXV" FT HELIX 59..70 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 77..82 FT /evidence="ECO:0007829|PDB:3DXV" FT HELIX 83..94 FT /evidence="ECO:0007829|PDB:3DXV" FT TURN 95..97 FT /evidence="ECO:0007829|PDB:3DXV" FT TURN 99..101 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 102..109 FT /evidence="ECO:0007829|PDB:3DXV" FT HELIX 110..125 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 129..133 FT /evidence="ECO:0007829|PDB:3DXV" FT HELIX 142..145 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 150..153 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 162..165 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:3DXV" FT HELIX 181..192 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 199..204 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 206..209 FT /evidence="ECO:0007829|PDB:3DXV" FT TURN 210..212 FT /evidence="ECO:0007829|PDB:3DXV" FT HELIX 220..230 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 234..238 FT /evidence="ECO:0007829|PDB:3DXV" FT TURN 240..242 FT /evidence="ECO:0007829|PDB:3DXV" FT TURN 244..247 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 248..251 FT /evidence="ECO:0007829|PDB:3DXV" FT HELIX 252..255 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 261..265 FT /evidence="ECO:0007829|PDB:3DXV" FT HELIX 267..270 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 276..281 FT /evidence="ECO:0007829|PDB:3DXV" FT HELIX 282..285 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 289..292 FT /evidence="ECO:0007829|PDB:3DXV" FT TURN 295..298 FT /evidence="ECO:0007829|PDB:3DXV" FT HELIX 300..315 FT /evidence="ECO:0007829|PDB:3DXV" FT HELIX 318..339 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 343..349 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 352..360 FT /evidence="ECO:0007829|PDB:3DXV" FT TURN 361..364 FT /evidence="ECO:0007829|PDB:3DXV" FT HELIX 368..381 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 386..389 FT /evidence="ECO:0007829|PDB:3DXV" FT STRAND 394..397 FT /evidence="ECO:0007829|PDB:3DXV" FT HELIX 405..420 FT /evidence="ECO:0007829|PDB:3DXV" FT HELIX 421..424 FT /evidence="ECO:0007829|PDB:3DXV" FT HELIX 427..431 FT /evidence="ECO:0007829|PDB:3DXV" SQ SEQUENCE 436 AA; 45699 MW; 85D1FC7936F7DDE5 CRC64; MTKALYDRDG AAIGNLQKLR FFPLAISGGR GARLIEENGR ELIDLSGAWG AASLGYGHPA IVAAVSAAAA NPAGATILSA SNAPAVTLAE RLLASFPGEG THKIWFGHSG SDANEAAYRA IVKATGRSGV IAFAGAYHGC TVGSMAFSGH SVQADAAKAD GLILLPYPDP YRPYRNDPTG DAILTLLTEK LAAVPAGSIG AAFIEPIQSD GGLIVPPDGF LRKFADICRA HGILVVCDEV KVGLARSGRL HCFEHEGFVP DILVLGKGLG GGLPLSAVIA PAEILDCASA FAMQTLHGNP ISAAAGLAVL ETIDRDDLPA MAERKGRLLR DGLSELAKRH PLIGDIRGRG LACGMELVCD RQSREPARAE TAKLIYRAYQ LGLVVYYVGM NGNVLEFTPP LTITETDIHK ALDLLDRAFS ELSAVSNEEI AQFAGW //