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Database: UniProt
Entry: E1TJR4_BURSG
LinkDB: E1TJR4_BURSG
Original site: E1TJR4_BURSG 
ID   E1TJR4_BURSG            Unreviewed;       389 AA.
AC   E1TJR4;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Aralkylamine dehydrogenase {ECO:0000313|EMBL:ADN59811.1};
DE            EC=1.4.9.2 {ECO:0000313|EMBL:ADN59811.1};
GN   OrderedLocusNames=BC1003_3872 {ECO:0000313|EMBL:ADN59811.1};
OS   Burkholderia sp. (strain CCGE1003).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN59811.1};
RN   [1] {ECO:0000313|EMBL:ADN59811.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN59811.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT   "Complete sequence of chromosome2 of Burkholderia sp. CCGE1003.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aromatic amine dehydrogenase heavy chain
CC       family. {ECO:0000256|ARBA:ARBA00010548}.
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DR   EMBL; CP002218; ADN59811.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1TJR4; -.
DR   STRING; 640512.BC1003_3872; -.
DR   KEGG; bgf:BC1003_3872; -.
DR   eggNOG; COG3391; Bacteria.
DR   HOGENOM; CLU_059384_0_0_4; -.
DR   OMA; WAPGGWQ; -.
DR   OrthoDB; 185182at2; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0030058; F:amine dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0030059; F:aralkylamine dehydrogenase (azurin) activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR009451; Metamine_DH_Hvc.
DR   InterPro; IPR011044; Quino_amine_DH_bsu.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR47197:SF3; DIHYDRO-HEME D1 DEHYDROGENASE; 1.
DR   PANTHER; PTHR47197; PROTEIN NIRF; 1.
DR   Pfam; PF06433; Me-amine-dh_H; 1.
DR   SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR609451-50};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Oxidoreductase {ECO:0000313|EMBL:ADN59811.1};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..389
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003152333"
FT   DISULFID        184..199
FT                   /evidence="ECO:0000256|PIRSR:PIRSR609451-50"
SQ   SEQUENCE   389 AA;  42019 MW;  9949CD486210F165 CRC64;
     MERRRRAVAR AASILALSYG LLACHAQAGA AEKPEELTVA KVPPVNPHRA FVVDVSFASM
     TDARVHVFDA DTSRFVGQID AGFAPGFSIS PDHKTSYVAT TYFSRGGHGT RTDVVELIDN
     ATLDIVGEIE IPVKHAQAVP TPYNTTLSDD GSRLYVSNIT PSTSVTVIDT SAKKVLGEID
     TDGCVLAYPS GNDRFTALCE SGKALTVKLD ATGKEVSRKL SDAFIDVEHD PAFVNAVRDG
     QRYLFTTFGG RVCSADFTGD TPVFGEPWSL VTSDERKAGW RPGGLQQTAF NAINQRLYVA
     MHQGSDGSHK DPATEVWVFD TVSKKRVARW KLAAQKIPPL LSIQVSADDK PLFYGLTPTS
     DFVVMDAATG KLRHVDKQLG TTSTLILNP
//
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