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Database: UniProt
Entry: A0A2H9U3R9_9GAMM
LinkDB: A0A2H9U3R9_9GAMM
Original site: A0A2H9U3R9_9GAMM 
ID   A0A2H9U3R9_9GAMM        Unreviewed;       389 AA.
AC   A0A2H9U3R9;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Heme biosynthesis protein HemY {ECO:0000313|EMBL:PJG58618.1};
GN   ORFNames=CUC53_11595 {ECO:0000313|EMBL:PJG58618.1};
OS   Aeromonas cavernicola.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=1006623 {ECO:0000313|EMBL:PJG58618.1, ECO:0000313|Proteomes:UP000235861};
RN   [1] {ECO:0000313|EMBL:PJG58618.1, ECO:0000313|Proteomes:UP000235861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MDC 2508 {ECO:0000313|EMBL:PJG58618.1,
RC   ECO:0000313|Proteomes:UP000235861};
RA   Colston S.M., Navarro A., Martinez-Murcia A.J., Graf J.;
RT   "Draft genome sequence of environmental isolate Aeromonas cavernicola sp.
RT   nov. MDC 2508.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in a late step of protoheme IX synthesis.
CC       {ECO:0000256|ARBA:ARBA00002962}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004744}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}.
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:PJG58618.1}.
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DR   EMBL; PGGC01000098; PJG58618.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H9U3R9; -.
DR   OrthoDB; 7067577at2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000235861; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042168; P:heme metabolic process; IEA:InterPro.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR005254; Heme_biosyn_assoc_TPR_pro.
DR   InterPro; IPR010817; HemY_N.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   NCBIfam; TIGR00540; TPR_hemY_coli; 1.
DR   Pfam; PF07219; HemY_N; 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
PE   4: Predicted;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        45..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          26..132
FT                   /note="HemY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07219"
SQ   SEQUENCE   389 AA;  43203 MW;  265AEB6D2270BE5F CRC64;
     MIRIIILVVV MVAGLIFGPH AAGNKGYVLV VLGDYTLESS VTSAVILAAL FYGALLITEW
     LLGRLFGLRR KTAGWYGSRR RRKANQQTVA ATLAMAEGHY SQAEKLMIKG ASNSDMPLLN
     YLSAAKAAQA RGDDARRDHY LQKAQEEHPK AELALALTQT QLQIEQGQYD AALATLEQLV
     ALHPRHPLLL DQLRQVYLAR QEWVALCNLI PTLHKAGKLT PKQEEELQQQ AWSGRLTQAA
     TTQASLQALW QELPRKLRQE PAMLACYGDL LCQLGADQEA ATLWQEVLRK QPAPQLLVRL
     PTLKLDNYQP LITLLQKQRG QPAVDSALAQ LYLLAGQLDD AQALLEQEIA QAPTAAAYHA
     LGQVMDKRRL TNKANEYYRH ALSLARPGY
//
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