ID   A0A060NH62_9BURK        Unreviewed;       180 AA.
AC   A0A060NH62;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Lactoylglutathione lyase and related lyase {ECO:0000313|EMBL:BAO81216.1};
GN   ORFNames=SRAA_1362 {ECO:0000313|EMBL:BAO81216.1};
OS   Serpentinimonas raichei.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Serpentinimonas.
OX   NCBI_TaxID=1458425 {ECO:0000313|EMBL:BAO81216.1, ECO:0000313|Proteomes:UP000067461};
RN   [1] {ECO:0000313|EMBL:BAO81216.1, ECO:0000313|Proteomes:UP000067461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1 {ECO:0000313|EMBL:BAO81216.1,
RC   ECO:0000313|Proteomes:UP000067461};
RX   PubMed=24845058; DOI=10.1038/ncomms4900;
RA   Suzuki S., Kuenen J.G., Schipper K., van der Velde S., Ishii S., Wu A.,
RA   Sorokin D.Y., Tenney A., Meng X.Y., Morrill P.L., Kamagata Y., Muyzer G.,
RA   Nealson K.H.;
RT   "Physiological and genomic features of highly alkaliphilic hydrogen-
RT   utilizing Betaproteobacteria from a continental serpentinizing site.";
RL   Nat. Commun. 5:3900-3900(2014).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954,
CC         ECO:0000256|RuleBase:RU000683};
CC   -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC       {ECO:0000256|ARBA:ARBA00008784, ECO:0000256|RuleBase:RU000683}.
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DR   EMBL; AP014568; BAO81216.1; -; Genomic_DNA.
DR   RefSeq; WP_045531638.1; NZ_AP014568.1.
DR   AlphaFoldDB; A0A060NH62; -.
DR   STRING; 1458425.SRAA_1362; -.
DR   KEGG; cbaa:SRAA_1362; -.
DR   HOGENOM; CLU_084417_1_1_4; -.
DR   OrthoDB; 9804944at2; -.
DR   Proteomes; UP000067461; Chromosome.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd06587; VOC; 1.
DR   Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 1.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR037523; VOC.
DR   InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2.
DR   PANTHER; PTHR21366; GLYOXALASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR21366:SF33; GLYOXALASE FAMILY PROTEIN; 1.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR   PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
DR   PROSITE; PS51819; VOC; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797,
KW   ECO:0000256|RuleBase:RU000683};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU000683};
KW   Iron {ECO:0000256|RuleBase:RU000683}; Lyase {ECO:0000313|EMBL:BAO81216.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000683};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067461}.
FT   DOMAIN          5..137
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
SQ   SEQUENCE   180 AA;  20697 MW;  FE4ACE901F011F00 CRC64;
     MTIERIHHVA YRCRDARETV NWYVQHLQMD FVLAIAEDRV PSTKAPDPYM HVFLDAGQGN
     VLAFFELPNS PEMGRDPHTP AWVQHIAFKV ESLAVLEETK ARLQAAGIEV IGPTDHTIFK
     SIYFFDPNGH RLELVADCAT PDMLQRLDAV KWPMLDEWAQ TRRAPKHAAW MHEQELKALD
//