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Database: UniProt
Entry: C6XQB5_HIRBI
LinkDB: C6XQB5_HIRBI
Original site: C6XQB5_HIRBI 
ID   C6XQB5_HIRBI            Unreviewed;       380 AA.
AC   C6XQB5;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=Amine dehydrogenase {ECO:0000313|EMBL:ACT60414.1};
GN   OrderedLocusNames=Hbal_2741 {ECO:0000313|EMBL:ACT60414.1};
OS   Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC   Hyphomonadaceae; Hirschia.
OX   NCBI_TaxID=582402 {ECO:0000313|EMBL:ACT60414.1, ECO:0000313|Proteomes:UP000002745};
RN   [1] {ECO:0000313|Proteomes:UP000002745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49814 / DSM 5838 / IFAM 1418
RC   {ECO:0000313|Proteomes:UP000002745};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
CC   -!- SIMILARITY: Belongs to the aromatic amine dehydrogenase heavy chain
CC       family. {ECO:0000256|ARBA:ARBA00010548}.
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DR   EMBL; CP001678; ACT60414.1; -; Genomic_DNA.
DR   RefSeq; WP_015828564.1; NC_012982.1.
DR   AlphaFoldDB; C6XQB5; -.
DR   STRING; 582402.Hbal_2741; -.
DR   KEGG; hba:Hbal_2741; -.
DR   eggNOG; COG3391; Bacteria.
DR   HOGENOM; CLU_059384_0_0_5; -.
DR   OMA; WAPGGWQ; -.
DR   OrthoDB; 7209000at2; -.
DR   Proteomes; UP000002745; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0030058; F:amine dehydrogenase activity; IEA:InterPro.
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   Pfam; PF06433; Me-amine-dh_H; 1.
DR   SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR609451-50};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002745};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..380
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002974109"
FT   DISULFID        174..190
FT                   /evidence="ECO:0000256|PIRSR:PIRSR609451-50"
SQ   SEQUENCE   380 AA;  41005 MW;  AF2CF4ACE0F70983 CRC64;
     MSLKSCALGA LIFLASPVGF AQEPIAPEEL TVEKEIPDGE NVYVLSSSWA GASSVLVLSA
     DDLSYKGNIP AGLTPQVAML PGNEEGYIVS AFAERMMYGP VSAYLQKFDV KTLAFEQEVE
     MLPRMAQVAA QVTVLALSSD GKWAFVQNAT PATSVSVVKL SSGEVVDEIP NPGCWGIYPS
     TSGSKYSTLC GDGAMVTYVI GSDGKFLRQK ASEPIFDVET KPLFSNAQRD GINLMFISYD
     GSVVTVSDEG TEAVLRDEWK FNEGIEGNWA PGGYELSAFN EPNGILFVLM HSDAKDGSHK
     NGAEEMWALD IKNKKVLYRS AVEHIVNISV NQAKDKPLVF GTDSHDSGLY KYEVDPEAKF
     AAKLTAEFDL KGVGYLVAEK
//
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