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Database: UniProt
Entry: K6CQU5_9BACI
LinkDB: K6CQU5_9BACI
Original site: K6CQU5_9BACI 
ID   K6CQU5_9BACI            Unreviewed;       491 AA.
AC   K6CQU5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=4-hydroxyphenylacetate-3-hydroxylase {ECO:0000313|EMBL:EKN62622.1};
GN   ORFNames=BABA_25201 {ECO:0000313|EMBL:EKN62622.1};
OS   Neobacillus bataviensis LMG 21833.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN62622.1, ECO:0000313|Proteomes:UP000006316};
RN   [1] {ECO:0000313|EMBL:EKN62622.1, ECO:0000313|Proteomes:UP000006316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX   PubMed=23087684;
RA   Heylen K., Keltjens J.;
RT   "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT   reduction in Bacillus.";
RL   Front. Microbiol. 3:371-371(2012).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKN62622.1}.
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DR   EMBL; AJLS01000183; EKN62622.1; -; Genomic_DNA.
DR   RefSeq; WP_007088029.1; NZ_AJLS01000183.1.
DR   AlphaFoldDB; K6CQU5; -.
DR   STRING; 1117379.BABA_25201; -.
DR   PATRIC; fig|1117379.3.peg.5219; -.
DR   eggNOG; COG2368; Bacteria.
DR   OrthoDB; 9785230at2; -.
DR   Proteomes; UP000006316; Unassembled WGS sequence.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.3140.10; 4-hydroxybutyryl-coa dehydratase, domain 1; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   InterPro; IPR004925; HpaB/PvcC/4-BUDH.
DR   InterPro; IPR024719; HpaB/PvcC/4-BUDH_C.
DR   InterPro; IPR024674; HpaB/PvcC/4-BUDH_N.
DR   PANTHER; PTHR36117; 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE-RELATED; 1.
DR   PANTHER; PTHR36117:SF3; 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE-RELATED; 1.
DR   Pfam; PF03241; HpaB; 1.
DR   Pfam; PF11794; HpaB_N; 1.
DR   PIRSF; PIRSF000331; HpaA_HpaB; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|PIRSR:PIRSR000331-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006316}.
FT   DOMAIN          5..273
FT                   /note="HpaB/PvcC/4-BUDH N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11794"
FT   DOMAIN          280..480
FT                   /note="HpaB/PvcC/4-BUDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03241"
FT   BINDING         149..151
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT   BINDING         155..158
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT   BINDING         192
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT   BINDING         455..458
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
SQ   SEQUENCE   491 AA;  56087 MW;  D90DCC3AD63CCA70 CRC64;
     MGIRTGEQYI NAVKSRKPEV WLEGRKVENI LDEPVLKQAV IEIAKLYDLQ HDPEYQEQIT
     HICEETGERV NNAFLVPRSY EDLIKRRTAF EAYAEATFGL MGRSPDFLNV VLTSLYSNAH
     FLEKYNPQWG ENIRDYYKYI RDNDLFLTHA IVNPQNDRRK SSHEQKDMFT HLGVVEETVD
     GLIVRGAKFL ATLAPVTDEV IIYTFPGFQP GDERYAISFA LPIDTPGLRI ICRESMQDGK
     RPLFDHPLAS RFEEIDALLV FKDVLIPWDR VFLYNNVEAA NLLYPKTGIA QQPSHQSAVR
     GLVKLQFAAE VAARLADSIG VDAYLHVQEK LGELFQSVET IRALLHAAEY EYETTPEGEV
     MPNGVTLETI RGHMPNMYPR AIEVMQILGA GGLLLSPTGA DFESEELRED LDRYYVGREG
     ISGVERVSIF KLAWDLCGEA FGQRLLQYER YYTGDPIRKK AIFYNNIKRN SKFDMVDEAL
     KVGQLKELSN K
//
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