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Database: UniProt
Entry: F7T4S6_9BURK
LinkDB: F7T4S6_9BURK
Original site: F7T4S6_9BURK 
ID   F7T4S6_9BURK            Unreviewed;       212 AA.
AC   F7T4S6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Methylamine utilization protein MauD {ECO:0000256|ARBA:ARBA00019076};
GN   ORFNames=AXXA_19742 {ECO:0000313|EMBL:EGP44700.1};
OS   Achromobacter insuavis AXX-A.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=1003200 {ECO:0000313|EMBL:EGP44700.1, ECO:0000313|Proteomes:UP000004853};
RN   [1] {ECO:0000313|EMBL:EGP44700.1, ECO:0000313|Proteomes:UP000004853}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AXX-A {ECO:0000313|EMBL:EGP44700.1,
RC   ECO:0000313|Proteomes:UP000004853};
RA   Bador J., Amoureux L., Neuwirth C.;
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be specifically involved in the processing, transport,
CC       and/or maturation of the MADH beta-subunit.
CC       {ECO:0000256|ARBA:ARBA00003475}.
CC   -!- PATHWAY: One-carbon metabolism; methylamine degradation.
CC       {ECO:0000256|ARBA:ARBA00004856}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:EGP44700.1}.
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DR   EMBL; AFRQ01000075; EGP44700.1; -; Genomic_DNA.
DR   RefSeq; WP_006393932.1; NZ_GL982453.1.
DR   AlphaFoldDB; F7T4S6; -.
DR   GeneID; 71021491; -.
DR   PATRIC; fig|1003200.3.peg.3924; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_091361_0_0_4; -.
DR   OrthoDB; 462848at2; -.
DR   UniPathway; UPA00895; -.
DR   Proteomes; UP000004853; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030416; P:methylamine metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR013478; MeN_DH_accessory.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR02661; MauD; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          48..192
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   212 AA;  23186 MW;  99D02EE2966BFCE4 CRC64;
     MEALIISNFL LWGVVLCLML VILALSRQIG VLYERVAPMG ALTMDKGPAV GEAAPRFELA
     DLLGRRLTIG ERGQHSQLLF FLSPTCPVCK KLLPILKSVA GTESAWLRIV LASDGEMPEH
     LAFYRQAGLE RFPYLLSTEL GMKFQISKLP YAVLIDESGV IRAKGLINSR EQLESLFTAK
     ELGVASVQEF LAGGALEETR ISRKENGNAL VG
//
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